Document Detail


Mutation Val235Ala weakens binding of the 33-kDa manganese stabilizing protein of photosystem II to one of two sites.
MedLine Citation:
PMID:  9092836     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The 33-kDa protein of the photosynthetic O2-evolving complex, also known as manganese stabilizing protein, contributes to the structural stability of the photosystem II tetranuclear Mn cluster and stimulates the water-oxidizing activity of this cluster. Quantification of extrinsic polypeptides in photosystem II has yielded data that support stoichiometries of either one or two copies of each protein per photosystem II reaction center. We recently described the cold-sensitive assembly of a mutant 33-kDa protein with a single amino acid replacement (Val235Ala) [Betts, S. D., Ross, J. R., Pichersky, E., & Yocum, C. F. (1996) Biochemistry 35, 6302-6307]. We have extended the characterization of this mutation. When photosystem II membranes depleted of the 33 kDa extrinsic protein are exposed to mixtures of wild type and Val235Ala manganese stabilizing protein, binding of the wild type protein is strongly preferred. If, however, protein containing the Val235Ala mutation is first bound to photosystem II only half of this protein (about 1 mol/mol of photosystem II reaction centers) is susceptible to displacement by the wild type protein, even after multiple exposures to the latter. These results support the conclusion that 2 mol of manganese stabilizing protein are bound per reaction center. Our data show as well that the mutant 33-kDa protein competes with the wild type protein for at least one of two binding sites on photosystem II and that the mutant protein binds tightly to only one of two sites. These results demonstrate that the two binding sites on photosystem II for the 33-kDa protein have different properties with respect to recognition and binding of this protein.
Authors:
S D Betts; J R Ross; E Pichersky; C F Yocum
Related Documents :
16473546 - Cp43-like chlorophyll binding proteins: structural and evolutionary implications.
21154656 - Vortex-assisted tryptic digestion.
8707056 - Chemistries and colors of bioluminescent reactions: a review.
7981196 - Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hyd...
14610326 - Proteomic identification of a large complement of rat urinary proteins.
12821516 - Regional heterogeneity of cellular prion protein isoforms in the mouse brain.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  36     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1997 Apr 
Date Detail:
Created Date:  1997-04-29     Completed Date:  1997-04-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4047-53     Citation Subset:  IM    
Affiliation:
Department of Biology, The University of Michigan, Ann Arbor 48109-1048, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Arabidopsis / metabolism
Binding Sites
Binding, Competitive
Electrophoresis, Polyacrylamide Gel
Mutation
Photosynthetic Reaction Center Complex Proteins / metabolism*
Photosystem II Protein Complex*
Protein Binding
Proteins / chemistry,  genetics*
Spinacia oleracea / metabolism
Temperature
Chemical
Reg. No./Substance:
0/Photosynthetic Reaction Center Complex Proteins; 0/Photosystem II Protein Complex; 0/Proteins; 0/photosystem II manganese-stabilizing protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.
Next Document:  Cytochrome c/cytochrome c peroxidase complex: effect of binding-site mutations on the thermodynamics...