Document Detail

The lipoproteins of cyanobacterial photosystem II.
MedLine Citation:
PMID:  21349737     Owner:  NLM     Status:  Publisher    
Photosystem II (PSII) complexes from cyanobacteria and plants perform water splitting and plastoquinone reduction and yet have a different complement of lumenal extrinsic proteins. Whereas PSII from all organisms has the PsbO extrinsic protein, crystal structures of PSII from cyanobacteria have PsbV and PsbU while green algae and higher plants instead contain the extrinsic PsbP and PsbQ subunits. Proteomic studies in Synechocystis sp. PCC 6803 identified three further extrinsic proteins in the thylakoid lumen that are associated with cyanobacterial PSII and these are predicted to attach to the thylakoid membrane via a lipidated N-terminus. These proteins are cyanobacterial homologues to the PsbP and PsbQ subunits as well as to Psb27, an additional extrinsic protein associated with "inactive" photosystems that lack the other extrinsic polypeptides. The PsbQ homologue is not present in Prochlorococcus species but otherwise these proteins have been identified in most cyanobacteria although our phylogenetic analyses identified some strains that lack an apparent motif for lipidation in one or other of these subunits. Over the past decade the physiological function of these additional lipoproteins has been investigated in several cyanobacterial strains and recently the structures for each have been solved. This review will evaluate the physiological and structural results obtained for these lipid-attached extrinsic proteins and in silico protein docking of these proteins to PSII centers will be presented.
Robert D Fagerlund; Julian J Eaton-Rye
Related Documents :
22322217 - Single-molecule pull-down for studying protein interactions.
21426127 - Finding order within disorder: elucidating the structure of proteins associated with ne...
16500727 - The antifungal protein afp secreted by aspergillus giganteus does not cause detrimental...
21349737 - The lipoproteins of cyanobacterial photosystem ii.
17337257 - A unified view of base excision repair: lesion-dependent protein complexes regulated by...
15684817 - Camptothecin induces the ubiquitin-like protein, isg15, and enhances isg15 conjugation ...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-4
Journal Detail:
Title:  Journal of photochemistry and photobiology. B, Biology     Volume:  -     ISSN:  1873-2682     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-2-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8804966     Medline TA:  J Photochem Photobiol B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 Elsevier B.V. All rights reserved.
Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Overexpression of interleukin-1? and interferon-? in type I thoracic aortic dissections and ascendin...
Next Document:  Chemiluminescence as a PDT light source for microbial control.