Updated on 2024/02/02

写真a

 
KURODA Hiroshi
 
Organization
Research Institute for Interdisciplinary Science Special-Appointment Assistant Professor
Position
Special-Appointment Assistant Professor
External link

Degree

  • 博士（理学） ( 1996.9   岡山大学 )

  • 修士（理学） ( 1993.3   岡山大学 )

  • 理学士 ( 1991.3   岡山大学 )

  • 博士（理学） ( 岡山大学 )

Research Interests

  • Gene expression

  • Molecular biology

  • Plant physiology

  • Photosynthesis

Research Areas

  • Life Science / Plant molecular biology and physiology

Education

  • Okayama University   自然科学研究科   生物資源科学専攻

    1993.4 - 1996.9

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  • Okayama University   理学研究科   生物学専攻

    1991.4 - 1993.3

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  • Okayama University   理学部   生物学科

    1987.4 - 1991.3

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Research History

  • 異分野基礎科学研究所   特別契約職員助教

    2019.12

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  • 異分野基礎科学研究所   特別契約職員講師

    2016.4 - 2019.11

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  • 岡山大学大学院自然科学研究科   特別契約職員助教

    2012.4 - 2016.3

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  • 名古屋市立大学大学院システム自然科学研究科   研究員

    2004.5 - 2012.3

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  • Waksman Institute, Rutgers, The State University of New Jersey   Research Associate

    2001.1 - 2004.2

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    Country：United States

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  • Waksman Institute, Rutgers, The State University of New Jersey   Postdoctoral Fellow

    1997.4 - 2000.9

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    Country：United States

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  • National Institute for Basic Biology

    1996.10 - 1997.3

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Professional Memberships

 

Papers

  • Characterization of Tryptophan Oxidation Affecting D1 Degradation by FtsH in the Photosystem II Quality Control of Chloroplasts

    Yusuke Kato, Hiroshi Kuroda, Shin-Ichiro Ozawa, Keisuke Saito, Vivek Dogra, Martin Scholz, Guoxian Zhang, Catherine de Vitry, Hiroshi Ishikita, Chanhong Kim, Michael Hippler, Yuichiro Takahashi, Wataru Sakamoto

    2023.7

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    Publisher：eLife Sciences Publications, Ltd  

    Light reaction of photosynthesis is one of the most important reactions for sustaining our environment. Photosystem II (PSII) is the initial site of photosynthetic electron transfer by water oxidation. Light in excess, however, causes the simultaneous production of singlet oxygen, a potent reactive oxygen species (ROS), leading to photo-oxidative damage in PSII. To maintain photosynthetic activity, the PSII reaction center protein D1, which is the primary target of unavoidable photo-oxidative damage, is efficiently degraded by FtsH protease. In PSII subunits, photo-oxidative modifications of several amino acids such as Trp have been indeed documented, whereas the linkage between such modifications and D1 degradation remains elusive. Here, we show that an oxidative post-translational modification of Trp residue at the N-terminal tail of D1 is correlated with D1 degradation by FtsH during high-light stress. We revealed that Arabidopsis mutant lacking FtsH2 had increased levels of oxidative Trp residues in D1, among which an N-terminal Trp-14 was distinctively localized in the stromal side. Further characterization of Trp-14 using chloroplast transformation in Chlamydomonas indicated that substitution of D1 Trp-14 to Phe, mimicking Trp oxidation enhanced FtsH-mediated D1 degradation under high light, although the substitution did not affect protein stability and PSII activity. Molecular dynamics simulation of PSII implies that both Trp-14 oxidation and Phe substitution cause fluctuation of D1 N-terminal tail. Furthermore, Trp-14 to Phe modification appeared to have an additive effect in the interaction between FtsH and PSII core in vivo. Together, our results suggest that the Trp oxidation at its N-terminus of D1 may be one of the key oxidations in the PSII repair, leading to processive degradation by FtsH.

    In photosynthetic organisms, maintenance of photosynthetic light reaction is manifested by so called Photosystem II (PSII) repair system, where the reaction center protein D1 is targeted to photo-oxidative damage and rapidly degraded by the processive protease FtsH. While this system is well known to cope with photoinhibition, the actual oxidation within the D1 polypeptide and its association to degradation remained elusive. Here, we characterized oxidative modification of tryptophan (Trp) residues in the PSII core, and hypothesize that the oxidation of N-terminal Trp is one of the key oxidations in the PSII repair, likely enhancing D1’s accessibility to FtsH.

    DOI： 10.7554/elife.88822.1

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  • Assembly Apparatus of Light-Harvesting Complexes; Identification of Alb3.1-cpSRP-LHCP Complexes in the Green Alga Chlamydomonas reinhardtii. Reviewed

    Mithun Kumar Rathod, Nellaipalli Sreedhar, Shin-Ichiro Ozawa, Hiroshi Kuroda, Natsumi Kodama, Sandrine Bujaldon, Francis-André Wollman, Yuichiro Takahashi

    Plant & cell physiology   2021.10

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    Language：English   Publishing type：Research paper (scientific journal)  

    The unicellular green alga, Chlamydomonas reinhardtii, contains many light-harvesting complexes (LHCs) associating chlorophylls a/b and carotenoids; the major light-harvesting complexes, LHCIIs (types I, II, III, and IV), and minor light-harvesting complexes, CP26 and CP29, for photosystem II, as well as nine light-harvesting complexes, LHCIs (LHCA1-9), for photosystem I. A pale green mutant BF4 exhibited impaired accumulation of LHCs due to deficiency in Alb3.1 gene which encodes the insertase involved in insertion, folding and assembly of LHC proteins in the thylakoid membranes. To elucidate the molecular mechanism by which ALB3.1 assists LHC assembly, we complemented BF4 to express ALB3.1 fused with no, single, or triple HA tag at its C-terminus (cAlb3.1, cAlb3.1-HA, or cAlb3.1-3HA). The resulting complemented strains accumulated most LHC proteins comparable to wild-type levels. The affinity purification of Alb3.1-HA and Alb3.1-3HA preparations showed that ALB3.1 interacts with cpSRP43 and cpSRP54 proteins of chloroplast signal recognition particle cpSRP and several LHC proteins; two major LHCII proteins (types I and III), two minor LHCII proteins (CP26 and CP29), and eight LHCI proteins (LHCA1, 2, 3, 4, 5, 6, 8, and 9). Pulse-chase labeling experiments revealed that the newly synthesized major LHCII proteins were transiently bound to the Alb3.1 complex. We propose that Alb3.1 interacts with cpSRP43 and cpSRP54 to form an assembly apparatus for most LHCs in the thylakoid membranes. Interestingly, PSI proteins were also detected in the Alb3.1 preparations, suggesting that the integration of LHCIs to a PSI core complex to form a PSI-LHCI subcomplex occurs before assembled LHCIs dissociate from the Alb3.1-cpSRP complex.

    DOI： 10.1093/pcp/pcab146

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  • Proton transfer pathway from the oxygen-evolving complex in photosystem II substantiated by extensive mutagenesis Reviewed International journal

    Hiroshi Kuroda, Keisuke Kawashima, Kazuyo Ueda, Takuya Ikeda, Keisuke Saito, Ryo Ninomiya, Chisato Hida, Yuichiro Takahashi, Hiroshi Ishikita

    Biochimica et Biophysica Acta (BBA) - Bioenergetics   1862 ( 1 )   148329 - 148329   2021.1

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    Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    We report a structure-based biological approach to identify the proton-transfer pathway in photosystem II. First, molecular dynamics (MD) simulations were conducted to analyze the H-bond network that may serve as a Grotthuss-like proton conduit. MD simulations show that D1-Asp61, the H-bond acceptor of H2O at the Mn4CaO5 cluster (W1), forms an H-bond via one water molecule with D1-Glu65 but not with D2-Glu312. Then, D1-Asp61, D1-Glu65, D2-Glu312, and the adjacent residues, D1-Arg334, D2-Glu302, and D2-Glu323, were thoroughly mutated to the other 19 residues, i.e., 114 Chlamydomonas chloroplast mutant cells were generated. Mutation of D1-Asp61 was most crucial. Only the D61E and D61C cells grew photoautotrophically and exhibit O2-evolving activity. Mutations of D2-Glu312 were less crucial to photosynthetic growth than mutations of D1-Glu65. Quantum mechanical/molecular mechanical calculations indicated that in the PSII crystal structure, the proton is predominantly localized at D1-Glu65 along the H-bond with D2-Glu312, i.e., pKa(D1-Glu65) > pKa(D2-Glu312). The potential-energy profile shows that the release of the proton from D1-Glu65 leads to the formation of the two short H-bonds between D1-Asp61 and D1-Glu65, which facilitates downhill proton transfer along the Grotthuss-like proton conduit in the S2 to S3 transition. It seems possible that D1-Glu65 is involved in the dominant pathway that proceeds from W1 via D1-Asp61 toward the thylakoid lumen, whereas D2-Glu312 and D1-Arg334 may be involved in alternative pathways in some mutants.

    DOI： 10.1016/j.bbabio.2020.148329

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  • The photosystem I assembly apparatus consisting of Ycf3–Y3IP1 and Ycf4 modules Reviewed

    Sreedhar Nellaepalli, Shin-Ichiro Ozawa, Hiroshi Kuroda, Yuichiro Takahashi

    Nature Communications   9 ( 1 )   2018.12

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1038/s41467-018-04823-3

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    Other Link： http://www.nature.com/articles/s41467-018-04823-3

  • Processing of the 5′-UTR and existence of protein factors that regulate translation of tobacco chloroplast psbN mRNA Reviewed

    Hiroshi Kuroda, Masahiro Sugiura

    Plant Molecular Biology   86 ( 6 )   585 - 593   2014.12

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1007/s11103-014-0248-z

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    Other Link： http://link.springer.com/article/10.1007/s11103-014-0248-z/fulltext.html

  • Requirement for Asn298 on D1 Protein for Oxygen Evolution: Analyses by Exhaustive Amino Acid Substitution in the Green Alga Chlamydomonas reinhardtii Reviewed

    Hiroshi Kuroda, Natsumi Kodama, Xiao-Yu Sun, Shin-ichiro Ozawa, Yuichiro Takahashi

    Plant and Cell Physiology   55 ( 7 )   1266 - 1275   2014.7

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/pcp/pcu073

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  • Translation of partially overlapping psbD-psbC mRNAs in chloroplasts: the role of 5′-processing and translational coupling Reviewed

    Yuka Adachi, Hiroshi Kuroda, Yasushi Yukawa, Masahiro Sugiura

    Nucleic Acids Research   40 ( 7 )   3152 - 3158   2012.4

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    Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/nar/gkr1185

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  • ppGpp inhibits peptide elongation cycle of chloroplast translation system in vitro Reviewed

    Yuhta Nomura, Taito Takabayashi, Hiroshi Kuroda, Yasushi Yukawa, Kwanchanok Sattasuk, Mitsuru Akita, Akira Nozawa, Yuzuru Tozawa

    Plant Molecular Biology   78 ( 1-2 )   185 - 196   2012.1

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1007/s11103-011-9858-x

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    Other Link： http://link.springer.com/article/10.1007/s11103-011-9858-x/fulltext.html

  • The downstream atpE cistron is efficiently translated via its own cis-element in partially overlapping atpB–atpE dicistronic mRNAs in chloroplasts Reviewed

    Haruka Suzuki, Hiroshi Kuroda, Yasushi Yukawa, Masahiro Sugiura

    Nucleic Acids Research   39 ( 21 )   9405 - 9412   2011.11

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    Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/nar/gkr644

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  • Translation of psbC mRNAs Starts from the Downstream GUG, not the Upstream AUG, and Requires the Extended Shine–Dalgarno Sequence in Tobacco Chloroplasts Reviewed

    Hiroshi Kuroda, Haruka Suzuki, Takahiro Kusumegi, Tetsuro Hirose, Yasushi Yukawa, Masahiro Sugiura

    Plant and Cell Physiology   48 ( 9 )   1374 - 1378   2007.9

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    Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/pcp/pcm097

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  • A new in vitro translation system for non-radioactive assay from tobacco chloroplasts: effect of pre-mRNA processing on translation in vitro Reviewed

    Maki Yukawa, Hiroshi Kuroda, Masahiro Sugiura

    The Plant Journal   49 ( 2 )   367 - 376   2007.1

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    Publishing type：Research paper (scientific journal)   Publisher：Wiley  

    DOI： 10.1111/j.1365-313x.2006.02948.x

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  • Gene activation in plastids by the CRE site-specific recombinase Reviewed

    Tarinee Tungsuchat, Hiroshi Kuroda, Jarunya Narangajavana, Pal Maliga

    Plant Molecular Biology   61 ( 4-5 )   711 - 718   2006.7

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1007/s11103-006-0044-5

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    Other Link： http://link.springer.com/article/10.1007/s11103-006-0044-5/fulltext.html

  • The plastid clpP1 protease gene is essential for plant development Reviewed

    Hiroshi Kuroda, Pal Maliga

    Nature   425 ( 6953 )   86 - 89   2003.9

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1038/nature01909

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    Other Link： http://www.nature.com/articles/nature01909

  • Expression of tetanus toxin Fragment C in tobacco chloroplasts Reviewed

    John S. Tregoning, Peter Nixon, Hiroshi Kuroda, Zora Svab, Simon Clare, Frances Bowe, Neil Fairweather, Jimmy Ytterberg, Klaas J. van Wijk, Gordon Dougan, Pal Maliga

    Nucleic Acids Research   31 ( 4 )   1174 - 1179   2003.2

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    Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/nar/gkg221

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  • Overexpression of the clpP 5′-Untranslated Region in a Chimeric Context Causes a Mutant Phenotype, Suggesting Competition for a clpP-Specific RNA Maturation Factor in Tobacco Chloroplasts Reviewed

    Hiroshi Kuroda, Pal Maliga

    Plant Physiology   129 ( 4 )   1600 - 1606   2002.8

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：American Society of Plant Biologists (ASPB)  

    DOI： 10.1104/pp.004986

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  • Complementarity of the 16S rRNA penultimate stem with sequences downstream of the AUG destabilizes the plastid mRNAs Reviewed

    Hiroshi Kuroda, Pal Maliga

    Nucleic Acids Research   29 ( 4 )   970 - 975   2001.2

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/nar/29.4.970

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  • Sequences Downstream of the Translation Initiation Codon Are Important Determinants of Translation Efficiency in Chloroplasts Reviewed

    Hiroshi Kuroda, Pal Maliga

    Plant Physiology   125 ( 1 )   430 - 436   2001.1

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：American Society of Plant Biologists (ASPB)  

    DOI： 10.1104/pp.125.1.430

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  • Possible Involvement of a Low Redox Potential Component(s) Downstream of Photosystem I in the Translational Regulation of the D1 Subunit of the Photosystem II Reaction Center in Isolated Pea Chloroplasts Reviewed

    Hiroshi Kuroda, Kumiko Kobashi, Hiroyuki Kaseyama, Kimiyuki Satoh

    Plant and Cell Physiology   37 ( 6 )   754 - 761   1996.9

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    Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    Accumulation of the precursor and the mature form of the D1 protein of the photosystem II reaction center in illuminated pea chloroplasts was prevented by the addition of the inhibitors atrazine, 3-(3,4-dichlorophenyl)-1,1-dimethylurea and 3,5-dibromo-4-hydroxybenzonitrile. Under such conditions, the compensatory accumulation of two translational intermediates of the D1 protein, of 22 and 24 kDa, respectively, was induced by the addition of ATP, as also observed in darkness in the presence of ATP [Taniguchi et al. (1993) FEBS Lett. 317: 57], suggesting that the synthesis of the full-length Dl protein requires a factor that is generated by the operation of photosynthetic electron transport. The accumulation of the full-length D1 protein was induced in the light, even in the presence of atrazine, when both 2,6-dichlorophenolindophenol and ascorbate were also present and in darkness upon the addition of dithiothreitol. Moreover, reagents with a relatively low redox potential, namely, duroquinone and methylviologen, prevented the accumulation. These observations suggest that the translation of the D1 protein might be regulated at specific steps during the elongation of the poly-peptide via a redox change in a component around photosystem I. Results of pre-illumination experiments indicate that the factor needed for the accmulation of D1 protein is relatively stable and retains its activity in darkness after exposure to light.

    DOI： 10.1093/oxfordjournals.pcp.a029010

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  • ATP-dependent protein synthesis in isolated pea chloroplasts Reviewed

    Michi Taniguchi, Hiroshi Kuroda, Kimiyuki Satoh

    FEBS Letters   317 ( 1-2 )   57 - 61   1993.2

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    Publishing type：Research paper (scientific journal)   Publisher：Wiley  

    DOI： 10.1016/0014-5793(93)81491-h

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  • The Level of Stromal ATP Regulates Translation of the D1 Protein in Isolated Chloroplasts Reviewed

    Hiroshi Kuroda, Noritoshi Inagaki, Kimiyuki Satoh

    Plant and Cell Physiology   33   33 - 39   1992.1

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    DOI： 10.1093/oxfordjournals.pcp.a078217

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MISC

  • 形質転換：タバコ：葉緑体ゲノム

    黒田洋詩

    低温科学（光合成研究法）   67   632 - 639   2009

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  • Chloroplasts for the production of recombinant proteins

    Pal Maliga, Hiroshi Kuroda

    PS2001 Proceedings: 12th International Congress on Photosynthesis   S40-001   2002

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  • Tobacco chloroplasts as a platform for vaccine production

    Pal Maliga, John Tregoning, Hiroshi Kuroda, Zora Svab, Kerry Lutz, Sylvie Corneille, Peter Nixon, Simon Clare, Frances Bowe, Neil Fairweather, Gordon Dougan

    Proc.10th IAPTC&B Congress (Plant Biotechnology 2002 and Beyond)   397 - 400   2002

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  • Accumulation of translational intermediates of the D1 protein in pea chloroplasts in the dark

    Hiroshi Kuroda, Kimiyuki Satoh

    Photosynthesis: from Light to Biosphere   III   1995

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    Authorship：Lead author  

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  • Mechanism of light-regulated synthesis of D1 protein in isolated chloroplasts

    Michi Taniguchi, Hiroshi Kuroda, Noritoshi Inagaki, Kimiyuki Satoh

    Research in Photosynthesis   III   1992

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Presentations

  • 集光性クロロフィルタンパク質の輸送に関与するcpSRP43タンパク質のアフィニティ精製

    黒田洋詩, 小澤真一郎, 濱尾志乃, 高橋裕一郎

    日本植物学会第86回大会  2022.9.17 

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    Event date： 2022.9.17 - 2022.9.19

    Language：Japanese   Presentation type：Oral presentation (general)  

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  • Chlamydomonas cpSRP consists of cpSRP43 and cpSRP54 and binds to ALB3.1 in the thylakoid membranes

    Hiroshi Kuroda, Shin-ichiro Ozawa, Shino Hamao, Yuichiro Takahashi

    2022.3.23 

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    Event date： 2022.3.22 - 2022.3.24

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  • 光化学系II酸素発生型近傍の水素結合ネットワークの機能解析

    黒田洋詩, 河島圭佑, 上田和世, 池田拓也, 斉藤圭亮, 二宮亮, 肥田千聖, 高橋裕一郎, 石北央

    第６１回植物生理学会年会  2020 

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  • 光化学系IIのキノン電子受容体近傍のアミノ酸置換による活性への影響

    黒田洋詩, 小松泰斗, 丹原瑠璃, 斉藤圭亮, 石北央, 高橋裕一郎

    日本植物学会第８４回大会  2020 

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  • Functional analysis of hydrogen bond networks in photosystem II by Chlamydomonas chloroplast transformation.

    Hiroshi Kuroda

    International Symposium "Photosynthesis Research for the Future"  2019 

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  • 緑藻クラミドモナスにおける光化学系II酸素発生系の水素結合ネットワークへの変異の影響

    黒田洋詩, 寺西知紘, 高橋裕一郎

    第10回光合成学会年会  2019 

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    Presentation type：Poster presentation  

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  • PSIIの水素結合ネットワークYZ経路はプロトン排出に関与するか？

    黒田洋詩, 兒玉なつ美, 孫小羽, 菓子野康浩, 高橋裕一郎

    第59回日本植物生理学会年会  2018 

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  • Asn298 on D1 subunit of photosystem II plays an important role on function of YZ in Chlamydomonas reinhardtii.

    Hiroshi Kuroda, Natsumi Kodama, Xiao-Yu Sun, Yasuhiro Kashino, Yuichiro Takahashi

    International Symposium on Photosynthesis and Chloroplast Biogenesis  2018 

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    Presentation type：Poster presentation  

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  • D1タンパク質のN298残基はYZの機能に重要である

    黒田洋詩, 兒玉なつ美, 孫小羽, 菓子野康浩, 高橋裕一郎

    第9回光合成学会年会  2018 

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  • 光化学系IIサブユニットへのアミノ酸置換と系II活性への影響

    黒田洋詩, 上田和世, 岡本真奈, 二宮亮, 肥田千聖, 高橋裕一郎

    日本植物学会第81回大会  2017 

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    Presentation type：Oral presentation (general)  

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  • PSII活性におけるD2タンパク質のR294残基の役割

    黒田洋詩, 岡本真奈, 高橋裕一郎

    第８回光合成学会年会  2017 

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  • 緑藻クラミドモナスの光化学系IIにおけるD2タンパク質のArg-294の役割

    黒田洋詩, 岡本真奈, 二宮亮, 肥田千聖, 高橋裕一郎

    第58回日本植物生理学会年会  2017 

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  • 緑藻クラミドモナスにおける D2 タンパク質の Arg-294 への変異導入の影響

    黒田洋詩, 岡本真奈, 高橋裕一郎

    第57回日本植物生理学会年会  2016 

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  • Mutation at Asn298 of D1 subunit on photosystem II impairs S state transition.

    Hiroshi Kuroda, Natsumi Kodama, Kazuyo Ueda, Yasuhiro Kashino, Yuichiro Takahashi

    17th International Conference on the Cell and Molecular Biology of Chlamydomonas  2016 

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  • 緑藻クラミドモナスにおける光化学系II反応中心D2タンパク質のR294への変異の影響

    黒田洋詩, 岡本真奈, 高橋裕一郎

    第７回光合成学会年会  2016 

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  • 緑藻クラミドモナスにおける光化学系IIサブユニットのアミノ酸置換と活性への影響

    黒田洋詩, 岡本真奈, 高橋裕一郎

    日本植物学会第79回大会  2015 

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  • クラミドモナス葉緑体形質転換による光化学系IIサブユニットのアミノ酸置換とその影響

    黒田洋詩, 岡本真奈, 高橋裕一郎

    第12回クラミドモナス研究会  2015 

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  • PSII反応中心D1サブユニットのAsn-298への変異導入と酸素発生活性への影響

    黒田洋詩, 兒玉なつ美, 上田和世, 孫小羽, 菓子野康浩, 高橋裕一郎

    第6回光合成学会年会  2015 

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  • 光化学系II反応中心D1タンパク質のAsn-298変異株の酸素発生活性の解析

    黒田洋詩, 兒玉なつ美, 上田和世, 孫小羽, 菓子野康浩, 高橋裕一郎

    第56回日本植物生理学会年会  2015 

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  • 系II反応中心D1タンパク質のAsn298のアミノ酸置換による酸素発生活性への影響

    黒田洋詩, 孫小羽, 兒玉なつ美, 小澤真一郎, 高橋裕一郎

    日本植物学会第78回大会  2014 

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  • Mutagenesis of D1-N298 impaired photosystem II activity in Chlamydomonas reinhardtii.

    Hiroshi Kuroda, Kodama Natsumi, Xiao-Yu Sun, Yuichiro Takahashi

    2014 

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  • 緑藻クラミドモナスD1タンパク質のAsn298のアミノ酸置換による酸素発生活性への影響

    黒田洋詩, 兒玉なつ美, 孫小羽, 小澤真一郎, 高橋裕一郎

    第22回光合成セミナー  2014 

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  • 緑藻クラミドモナスにおけるD1タンパク質のアミノ酸置換によるPSII活性への影響

    黒田洋詩, 兒玉なつ美, 孫小羽, 小澤真一郎, 高橋裕一郎

    第5回日本光合成学会年会および公開シンポジウム  2014 

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  • 緑藻クラミドモナス光化学系IIサブユニットD1のN298への部位特異的変異導入

    黒田洋詩, 兒玉なつ美, 孫小羽, 小澤真一郎, 高橋裕一郎

    第71回中国四国植物学会  2014 

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  • Engineering of a potential proton exit channel of photosystem II oxygen-evolving center in Chlamydomonas reinhardtii

    Hiroshi Kuroda, Xiao-Yu Sun, Natsumi Kodama, Yuichiro Takahashi

    2013 

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  • 酸素発生系プロトン排出経路の同定へ向けた光化学系IIサブユニットのエンジニアリング

    黒田洋詩, 高橋裕一郎

    日本植物学会第77回大会  2013 

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  • 緑藻クラミドモナス葉緑体形質転換法による光化学系 II サブユニットのエンジニアリング

    黒田洋詩, 孫小羽, 兒玉なつ美, 高橋裕一郎

    第４回日本光合成学会年会および公開シンポジウム  2013 

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  • タバコ葉緑体 psbD-psbC にみられる翻訳共役

    足立由佳, 黒田洋詩, 湯川泰, 杉浦昌弘

    日本植物生理学会第52回年会  2011 

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  • タバコ葉緑体 psbD-psbC 発現における翻訳開始機構の解析

    足立由佳, 黒田洋詩, 湯川泰, 杉浦昌弘

    第34回日本分子生物学会年会  2011 

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  • タバコ葉緑体 psbD-psbC 発現にみられる翻訳共役

    足立由佳, 黒田洋詩, 湯川泰, 杉浦昌弘

    日本光合成学会第２回年会および公開シンポジウム  2011 

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  • Translation of chloroplast rps2 mRNA is facilitated by a ribosomal protein S1.

    Hiroshi Kuroda, Shin-ichiro Ozawa, Yuichiro Takahashi, Yuka Adachi, Yasushi Yukawa, Masahiro Sugiura

    International Symposium on Biodiversity Sciences "Genome, Evolution and Environment"  2010 

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  • Requirements for translation initiation of rps2 mRNA in tobacco chloroplasts.

    Hiroshi Kuroda, Yuka Adachi, Shin-ichiro Ozawa, Yuichiro Takahashi, Yasushi Yukawa, Masahiro Sugiura

    2010 

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  • 葉緑体翻訳開始に関与するトランス因子

    黒田洋詩, 杉浦昌弘

    日本植物生理学会第50回年会  2009 

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  • 葉緑体 clpP1 mRNA の翻訳開始機構の解析

    黒田洋詩, 杉浦昌弘

    第32回日本分子生物学会年会  2009 

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  • 葉緑体 in vitro 翻訳系を用いた atpE mRNA 翻訳開始機構の解析

    黒田洋詩, 鈴木晴香, 湯川泰, 杉浦昌弘

    日本植物生理学会第49回年会  2008 

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  • 葉緑体 mRNA の翻訳開始に必要なシス配列とトランス因子

    黒田洋詩, 杉浦昌弘

    第31回日本分子生物学会年会・第81回日本生化学会大会 合同大会  2008 

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  • An active in vitro translation system from chloroplasts: a powerful tool to study mechanism of translation in chloroplasts

    Hiroshi Kuroda, Maki Yukawa, Haruka Suzuki, Yasushi Yukawa, Masahiro Sugiura

    IPR Seminar 2008 "The Ins and Outs of Chloroplasts"  2008 

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  • SD 様配列を持たない葉緑体 mRNA の翻訳開始機構の解析

    黒田洋詩, 杉浦昌弘

    第30回日本分子生物学会・第80回日本生化学会 合同年会  2007 

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  • 葉緑体 in vitro 翻訳系を用いた葉緑体 psbN mRNA 翻訳開始機構の解析

    黒田洋詩, 杉浦昌弘

    第48回日本植物生理学会年会  2007 

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  • 光化学系IIサブユニットCP43をコードするタバコ葉緑体psbCの翻訳開始点はGUGである

    黒田洋詩, 鈴木晴香, 久寿米木幸寛, 廣瀬哲郎, 湯川泰, 杉浦昌弘

    日本光合成研究会・公開シンポジウム  2007 

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  • タバコ葉緑体の SD 様配列のない mRNA の翻訳開始に必要なシス領域とトランス因子の解析

    黒田洋詩, 杉浦昌弘

    第71回日本生化学会中部支部例会・シンポジウム  2007 

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  • 葉緑体 in vitro 翻訳系を用いた葉緑体翻訳機構の解析

    黒田洋詩, 湯川眞希, 杉浦昌弘

    第47回日本植物生理学会年会  2006 

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  • 葉緑体 in vitro 翻訳系を用いた葉緑体翻訳開始に関与するシス領域とトランス因子の解析

    黒田洋詩, 杉浦昌弘

    日本分子生物学会2006フォーラム  2006 

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  • 改良型葉緑体 in vitro 翻訳系を用いた葉緑体翻訳機構の解析

    黒田洋詩, 湯川眞希, 杉浦昌弘

    第28回日本分子生物学会年会  2005 

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  • Deletion of clpP1 prevents development of the tobacco shoot system identifying clpP1 as an essential plastid housekeeping gene.

    Hiroshi Kuroda, Pal Maliga

    7th International Congress of Plant Molecular Biology  2003 

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  • Chloroplasts for the production of recombinant proteins.

    Hiroshi Kuroda, Zora Svab, John Tregoning, Peter Nixon, Simon Clare, Frances Bowe, Gordon Dougan, Pal Maliga

    Plant Molecular Biology, New York Area Meeting  2002 

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  • Over-expression of the clpP 5'UTR in a chimeric context confers a mutant phenotype by interference with maturation of clpP mRNA.

    Hiroshi Kuroda, Pal Maliga

    The Annual Meeting of the American Society of Plant Physiologists  2000 

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  • The role of downstream box sequence in plastid mRNA translation.

    Hiroshi Kuroda, Pal Maliga

    EMBO Workshop  1999 

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  • The role of the downstream box in the translation of plastid mRNAs.

    Hiroshi Kuroda, Pal Maliga

    XIth International Congress on Photosynthesis  1998 

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  • 光化学系II反応中心D1蛋白質合成における翻訳制御の分子機構

    黒田洋詩, 小橋久美子, 佐藤公行

    第3回日本光生物学協会講演会  1996 

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  • 光化学系II反応中心D1蛋白質の翻訳における"redox"制御

    黒田洋詩, 小橋久美子, 佐藤公行

    日本植物学会中四国支部第53回大会  1996 

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  • In vitro 翻訳系を用いたエンドウD1蛋白質合成の光制御機構の解析

    黒田洋詩, 小橋久美子, 佐藤公行

    日本植物生理学会1996年度年会および第36回シンポジウム  1996 

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  • Accumulation of translational intermediates of D1 protein in pea chloroplasts in the dark.

    Hiroshi Kuroda, Kimiyuki Satoh

    The Xth International Photosynthesis Congress  1995 

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  • エンドウ葉緑体におけるD1タンパク質翻訳中間体蓄積機構の解析

    黒田洋詩, 佐藤公行

    日本植物学会第59回大会  1995 

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  • エンドウ単離葉緑体を用いたD1タンパク質合成の光による制御機構の解析

    黒田洋詩, 忰山博之, 佐藤公行

    日本植物生理学会1994年度年会および第34回シンポジウム  1994 

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  • Accumulation of translation intermediates of D1 protein in isolated pea chloroplasts in the dark.

    Hiroshi Kuroda, Kimiyuki Satoh

    The 34th NIBB Conference  1994 

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    Presentation type：Symposium, workshop panel (public)  

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  • 光化学系II反応中心D1タンパク質の光による合成制御の機構

    黒田洋詩, 忰山博之, 佐藤公行

    日本植物学会中四国支部第50回大会  1993 

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  • D1蛋白質合成の光による制御の機構−クラミドモナス生細胞を用いた解析−

    黒田洋詩, 佐藤公行

    日本植物生理学会1992年度年会および第32回シンポジウム  1992.3 

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  • Mechanism of light-regulated synthesis of D1 protein in isolated chloroplasts

    Michi Taniguchi, Hiroshi Kuroda, Noritoshi Inagaki, Kimiyuki Satoh

    The IXth International Congress on Photosynthesis  1992 

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  • 単離葉緑体によるD1蛋白質の合成

    谷口三知, 黒田洋詩, 稲垣言要, 佐藤公行

    日本植物学会中四国支部第49回大会  1992 

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  • エンドウ単離葉緑体によるD1タンパク質の合成

    谷口三知, 黒田洋詩, 稲垣言要, 佐藤公行

    日本植物学会第57回大会  1992 

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  • 単離葉緑体におけるD1蛋白質合成の光による制御の機構

    黒田洋詩, 稲垣言要, 佐藤公行

    日本植物学会中四国支部第48回大会  1991 

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  • 単離葉緑体におけるD1蛋白質合成の光制御の機構

    黒田洋詩, 稲垣言要, 佐藤公行

    日本植物学会第56回大会  1991 

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Industrial property rights

  • Translation control elements for high-level protein expression in the plastids of higher plants and methods of use thereof.

    Pal Maliga, Hiroshi Kuroda, Muhammad Sarwar Khan

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    Application no：特願US 6,987,215 B1  Date applied：1999.8.3

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Research Projects

  • Study on PSII hydrogen bond networks by exhaustive amino acid substitution

    Grant number：15K07110  2015.04 - 2018.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    Kuroda Hiroshi

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    Authorship：Principal investigator 

    Grant amount：\5200000 （ Direct expense: \4000000 、 Indirect expense：\1200000 ）

    In oxygenic photoynthesis, there are several hydrogen bond networks between Mn cluster and lumen. To study role of these hydrogen bond networks, we have transformed Chlamydomonas chloroplast to substitute the participating amino acid residues of chloroplast-encoded PSII subunits with 19 other amino acids. We have examined their photosynthetic growth, PSII accumulation and activity. Analysis of the resulting transformants, we found that one of the hydrogen bond networks including D1-D61, D1-E65 and D2-E312 could be involved in excretion of protons generated during water oxidation at the Mn cluster. One of the hydrogen bond networks starting from YZ does not seem to be proton exit pathway.

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  • 葉緑体の正常な機能を支える翻訳制御機構の研究

    Grant number：24510267  2012

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    黒田 洋詩

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    Authorship：Principal investigator 

    Grant amount：\5460000 （ Direct expense: \4200000 、 Indirect expense：\1260000 ）

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  • Study of translational regulation of chloroplast mRNAs in response to environment

    Grant number：20570043  2008 - 2010

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    KURODA Hiroshi

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    Authorship：Principal investigator 

    Grant amount：\4940000 （ Direct expense: \3800000 、 Indirect expense：\1140000 ）

    The chloroplast is a site of photosynthesis, which produces carbohydrates and oxygen with solar energy. We have analyzed translation of several chloroplast genes and found variable important sequences among mRNA species, significance of mRNA processing and translational coupling of several genes. We also identified possible proteins for translational regulation in chloroplasts.

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  • Search for mRNA elements involved in the compatibility between 5' untranslated regions and coding regions in chloroplast translation

    Grant number：19370021  2007 - 2008

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)  Grant-in-Aid for Scientific Research (B)

    SUGIURA Masahiro, KURODA Hiroshi, NAKAMURA Masayuki, YUKAWA Maki

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    Authorship：Collaborating Investigator(s) (not designated on Grant-in-Aid) 

    Grant amount：\15730000 （ Direct expense: \12100000 、 Indirect expense：\3630000 ）

    植物細胞の中で光合成を行う葉緑体は盛んにタンパク質も作っている。そこで、葉緑体で有用タンパク質を生産する試みがなされたが、必ずしも成功しなかった。このことは、葉緑体のタンパク質合成の機構が動・植物の細胞質や細菌の機構とは違っていることを意味する。本研究で、葉緑体でのタンパク質合成にはメッセンジャーRNAの上流部分のみならずタンパク質のアミノ酸配列を規定する部分の一部も必要なことを明らかにした。

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  • Site-recognition of RNA editing in chloroplasts

    Grant number：17370020  2005 - 2006

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)  Grant-in-Aid for Scientific Research (B)

    SUGIURA Masahiro, YUKAWA Yasushi, NAKAMURA Masayuki, KURODA Hiroshi

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    Authorship：Coinvestigator(s) 

    Grant amount：\11500000 （ Direct expense: \11500000 ）

    1. RNA editing sites
    (1) Two additional sites were identified in the ndhD mRNA from tobacco (N. tabacum) chloroplasts. The total number of sites is thus 38, the most so far found in higher plant chloroplasts.
    (2) ACG to AUG RNA editing in ndhD mRNAs from tobacco progenitors (N sylvestris and N. tomentosiformis) was reexamined, and this editing in the latter species occurred depending on culture conditions.
    2. Improvement of the in vitro RNA editing assay
    A rapid and simple in vitro assay was established using fluorescent dideoxynucleotides.
    3. Cis-elements for RNA editing
    Using the above assay, editing activities of 19 sites in five tobacco ndh mRNA species were measured. A cis-element in the ndhB mRNA was defined to be 5 nucleotides (nt) from-6 to-10, whereas ndhF mRNAs have two separate cis-elements, 15 nt from-1 to-15 and 5 nt from-36 to-40.
    4. Trans-factors
    Using fuorescent mRNAs, a method to detect trans-factors for editing was tried.
    5. Analysis of site-recognition factors
    The 56 kD trans-factor for psbE mRNA editing was isolated, and its partial amino acid sequences were determined. No similar sequence was found in databases.

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