Faculty Profiles - SHEN Jian-Ren

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Low pH-Induced Dissociation of Three Extrinsic Proteins from O_2-Evolving Photosystem II :

Shen Jian-Ren, Inoue Yorinao

Plant and cell physiology 32 ( 3 ) 453 - 457 1991

Language：English Publisher：Japanese Society of Plant Physiologists

Three extrinsic proteins involved in oxygen evolution reversibly dissociated from Photo-system II (PS II) membranes at acidic pHS showing distinctly different pH dependencies. The pHS for half dissociation of 17, 23 and 33 kDa extrinsic proteins were determined to be 5.0, 4.1 and 3.6, respectively. The half dissociation pHS Of 17 and 23 kDa proteins were much lower than their respective isoelectric points, while that for 33 kDa protein was close to its isoelectric point. It was suggested that protonation of the negatively charged binding domain on membrane proteins causes dissociation of the former two extrinsic proteins, whereas protonation of the extrinsic protein itself is responsible for the dissociation of 33 kDa protein. Based on these, features of low pH-induced dissociation of extrinsic proteins and Mn from PS II were discussed.

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Other Link： https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=181397

Inactivation and Calcium-Dependent Reactivation of Oxygen Evolution in Photosystem II Preparations Treated at pH 3.0 or with High Concentrations of NaCl :

Shen Jian-Ren, Katoh Sakae

Plant and cell physiology 32 ( 3 ) 439 - 446 1991

Language：English Publisher：Japanese Society of Plant Physiologists

A brief treatment at pH 3.0 of Photosystem II (PS II) membranes containing two bound Ca^<2+> from rice resulted in strong suppression of oxygen evolution concomiiant with extraction of one Ca^<2+> and the lost activity was restored on addition of 50 mM Ca^<2+>. However, inactivation of oxygen evolution by low pH-treatment of oxygen-evolving PS II complexes containing only one Ca^<2+> from a rice chlorophyll b-deficient mutant was not associated with extraction of the bound Ca^<2+>, although oxygen evolution was markedly enhanced by the addition of Ca^<2+> to the treated complexes. Thus, the acid-inactivation of oxygen evolution cannot be related to extraction of Ca^<2+>. On the other hand, low pH-treatment was found to share the following common features with NaCl-treatment which also causes a Ca^<2+>-reversible inactivation of oxygen evolution. (1) Exposure of PS II membranes to pH 3.0 resulted in solubilization of the 23 and 17 kDa extrinsic proteins, although the released proteins rebound to the membranes when pH was raised to 6.5. (2) There was an apparent heterogeneity in the binding affinity of Ca^<2+> effective in restoration of the oxygen-evolving activity. (3) Low pH-treated preparations required a higher concentration of Ca^<2+> for the maximum reactivation of oxygen evolution than did NaCl-washed preparations. This was also the case with Sr^<2+>, which stimulated oxygen evolution of both low pH-treated and NaCl-washed PS II membranes to smaller extents. When the extrinsic 23 and 17 kDa proteins had been removed, however, Ca^<2+> concentration dependence of oxygen evolution in low pH-treated membranes became similar to that in NaCl-washed PS 11 preparations and the changes were largely reversed by rebinding of the two proteins. These results strongly suggest that low pH-treatment and NaCl-wash involve similar mechanisms of Ca^<2+>-dependent reactivation.

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Other Link： https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=181395

Isolation and characterization of Photosystem II complexes which lack light-harvesting chlorophyll a/b proteins but retain three extrinsic proteins related to oxygen evolution from spinach

Isao Enami, Kei Kamino, Jian-Ren Shen, Kazuhiko Satoh, Sakae Katoh

BBA - Bioenergetics 977 ( 1 ) 33 - 39 1989.10

Language：English

Oxygen-evolving Photosystem II (PS II) complexes, which were largely deprived of major light-harvesting chlorophyll a/b proteins (LHC II) but still associated with the 33 kDa, 23 kDa and 17 kDa extrinsic proteins related to oxygen evolution, were isolated from spinach oxygen-evolving PS II membranes with a non-ionic detergent, n-heptyl thioglucoside. A minor antenna chlorophyll-protein (CP 29) was present but in reducted amounts. The complexes contained all the constituent subunits of PS II reaction center core complexes, the 47 kDa and 43 kDa chlorophyll-carrying proteins, the D1 and D2 proteins and cytochrome b-559. In addition, three hydrophobic proteins of 29 kDa (CP 29 apoprotein), 20 kDa and 10 kDa were present. The antenna size was 80 chlorophyll a per QA, or 76 chlorophyll a per 4 Mn, and the complexes contained about 1 Ca2+ per PS II. With phenyl- or dichloro-p-benzoquinone as electron acceptor, the complexes showed high rates of oxygen evolution in the absence of exogenously added Ca2+. The activity became, however, strongly Ca2+-dependent when the 23 kDa and 17 kDa proteins, but not the bound Ca2+, had been removed with 1.5 M NaCl. The Ca2+ requirement disappeared on reconstitution of the complexes with the two proteins. The complexes were compared with other oxygen-evolving preparations having different polypeptide compositions and functions of several subunit proteins and Ca2+ in PS II electron transport are discussed. © 1989 Elsevier Science Publishers.

DOI： 10.1016/S0005-2728(89)80006-4

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Nearest neighbor relationships among constituent proteins of oxygen-evolving Photosystem II membranes: binding and function of the extrinsic 33 kDa protein

Isao Enami, Takeshi Miyaoka, Yasuki Mochizuki, Jian-Ren Shen, Kazuhiko Satoh, Sakae Katoh

BBA - Bioenergetics 973 ( 1 ) 35 - 40 1989

Language：English

Nearest neighbor relationships among constituent proteins of oxygen-evolving Photosystem II (PS II) membrane preparations from spinach were investigated by means of crosslinking with a cleavable bifunctional crosslinker, dithiobis(succinimidylpropionate) (DSP). (1) Diagonal gel electrophoresis revealed crosslinking between two extrinsic proteins of 17 and 23 kDa, between the extrinsic 33 kDa protein and the 47 kDa chlorophyll-carrying protein and between the 26 and 27 kDa apoproteins of light-harvesting chlorophyll a/b protein. In addition, a product which involved a protein of 29 kDa was detected. (2) Amounts of the extrinsic proteins crosslinked were determined by washing DSP-treated membranes with high concentrations of urea and NaCl, or CaCl2. Neither of the two extrinsic proteins of 17 and 23 kDa was crosslinked with intrinsic membrane proteins, whereas 15 to 20% of the 33 kDa protein was immobilized by treatment with 0.1% DSP. Oxygen evolution became resistant to the urea/NaCl-wash proportionally to the amount of the 33 kDa protein crosslinked, indicating that the 33 kDa protein covalently bound to the 47 kDa protein is still fully functional. (3) The crosslinking of the 33 kDa protein accompanied by parallel increases in the amount of Mn remained unextracted, and the rate of oxygen evolution survived after 30-min treatment of PS IImembranes at pH 9.0. Thus the 33 kDa protein has a protective effect on the Mn cluster at the alkaline pH. In contrast, Mn was mostly extracted with a high concentration of Tris, irrespective of the crosslinking of the 33 kDa protein. © 1989 Elsevier Science Publishers B.V. (Biomedical Division) All rights reserved.

DOI： 10.1016/S0005-2728(89)80399-8

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Calcium content of oxygen-evolving photosystem II preparations from higher plants. Effects of NaCl treatment.

SHEN J. R.

Biochim. Biophys. Acta 993 358 - 364 1988

Isolation of an oxygen-evolving photosystem II preparation containing only one tightly bound calcium atom a chlorophyII b-deficient mutant of rice.

SHEN J. -R.

Biochim. Biophys. Acta 936 386 - 394 1988

1Ca07 LHCPのない酸素発生系II標品の調整と諸性質

榎並勲, 紙野圭, 沈建仁, 佐藤和彦, 加藤栄

日本植物生理学会年会およびシンポジウム : 講演要旨集 28 55 - 55 1988

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