NDLI: Light- and pH-dependent structural changes in the PsbS subunit of photosystem II.

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Light- and pH-dependent structural changes in the PsbS subunit of photosystem II.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Segalla, Anna Teardo, Enrico Giacometti, Giorgio Mario Bergantino, Elisabetta Szabò, Ildikò Rigoni, Fernanda Brunetta, Alessia
Description	Author Affiliation: Bergantino E ( Department of Biology, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy.);
Abstract	In higher plants, the PsbS subunit of photosystem II (PSII) plays a crucial role in pH- and xanthophyll-dependent nonphotochemical quenching of excess absorbed light energy, thus contributing to the defense mechanism against photoinhibition. We determined the amino acid sequence of Zea mays PsbS and produced an antibody that recognizes with high specificity a region of the protein located in the stroma-exposed loop between the second and third putative helices. By means of this antiserum, the thylakoid membranes of various higher plant species revealed the presence of a 42-kDa protein band, indicating the formation of a dimer of the 21-kDa PsbS protein. Crosslinking experiments and immunoblotting with other antisera seem to exclude the formation of a heterodimer with other PSII protein components. The PsbS monomer/dimer ratio in isolated thylakoid membranes was found to vary with luminal pH in a reversible manner, the monomer being the prevalent form at acidic and the dimer at alkaline pH. In intact chloroplasts and whole plants, dimer-to-monomer conversion is reversibly induced by light, known to cause luminal acidification. Sucrose-gradient centrifugation revealed a prevalent association of the PsbS monomer and dimer with light-harvesting complex and PSII core complexes, respectively. The finding of the existence of a light-induced change in the quaternary structure of the PsbS subunit may contribute to understanding the mechanism of PsbS action during nonphotochemical quenching.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hydrogen-Ion Concentration Photosynthetic Reaction Center Complex Proteins Chemistry Photosystem II Protein Complex Plant Proteins Amino Acids Blotting, Western Centrifugation, Density Gradient Chloroplasts Metabolism Cloning, Molecular Cross-Linking Reagents Pharmacology DNA, Complementary Dimerization Gene Library Glutathione Transferase Models, Biological Molecular Sequence Data Precipitin Tests Protein Conformation Protein Structure, Quaternary Sucrose Thylakoids Zea Mays Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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