NDLI: High sensitivity proteomics assisted discovery of a novel operon involved in the assembly of photosystem II, a membrane protein complex.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Thornton, Leeann E. Monroe, Matthew E. Keren, Nir Hixson, Kim K. Camp, David G. Pakrasi, Himadri B. Welsh, Eric A. Wegener, Kimberly M. Jacobs, Jon M. Smith, Richard D.
Description	Author Affiliation: Wegener KM ( Department of Biology, Washington University, St. Louis, Missouri 63130, USA.)
Abstract	Photosystem II (PSII) is a large membrane protein complex that performs the water oxidation reactions of photosynthesis in cyanobacteria, algae, and plants. The unusual redox reactions in PSII often lead to damage, degradation, and reassembly of this molecular machine. To identify novel assembly factors, high sensitivity proteomic analysis of PSII purified from the cyanobacterium Synechocystis sp. PCC 6803 was performed. This analysis identified six PSII-associated proteins that are encoded by an operon containing nine genes, slr0144 to slr0152. This operon encodes proteins that are not essential components of the PSII holocomplex but accumulate to high levels in pre-complexes lacking any of the lumenal proteins PsbP, PsbQ, or PsbV. The operon contains genes with putative binding domains for chlorophylls and bilins, suggesting these proteins may function as a reservoir for cofactors needed during the PSII lifecycle. Genetic deletion of this operon shows that removal of these protein products does not alter photoautotrophic growth or PSII fluorescence properties. However, the deletion does result in decreased PSII-mediated oxygen evolution and an altered distribution of the S states of the catalytic manganese cluster. These data demonstrate that the proteins encoded by the genes in this operon are necessary for optimal function of PSII and function as accessory proteins during assembly of the PSII complex. Thus, we have named the products of the slr0144-slr0152 operon Pap (Photosystem II assembly proteins).
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	41
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-10-10
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism Membrane Proteins Operon Physiology Photosynthesis Photosystem II Protein Complex Synechocystis Genetics Chlorophyll Phycobilins Protein Binding Protein Structure, Tertiary Proteomics Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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