Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on June 24, 2005; 10.1104/pp.105.061549

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow Supplemental Data
Right arrow All Versions of this Article:
138/3/1586    most recent
pp.105.061549v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (3)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Xu, D.
Right arrow Articles by Zhao, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Xu, D.
Right arrow Articles by Zhao, J.
Agricola
Right arrow Articles by Xu, D.
Right arrow Articles by Zhao, J.

Received February 17, 2005
Returned for revision March 28, 2005
Accepted April 6, 2005

FesM, a Membrane Iron-Sulfur Protein, Is Required for Cyclic Electron Flow around Photosystem I and Photoheterotrophic Growth of the Cyanobacterium Synechococcus sp. PCC 7002

Dongyi Xu , Xianwei Liu , Jiao Zhao , and Jindong Zhao *

State Key Laboratory of Protein and Genetic Engineering, College of Life Science, Peking University, Beijing 100871, China

* Corresponding author; email: jzhao{at}pku.edu.cn.

While it is known that cyclic electron flow around photosystem I is an important pathway of photosynthetic electron transfer for converting light energy to chemical energy, some components of cyclic electron flow remain to be revealed. Here, we show that fesM, encoding a novel membrane iron-sulfur protein, is essential to cyclic electron flow in the cyanobacterium Synechococcus sp. PCC 7002. The FesM protein is predicted to have a cAMP-binding domain, an NtrC-like domain, a redox sensor motif, and an iron-sulfur (4Fe-4S) motif. Deletion of fesM (fesM-D) led to an inability for Synechococcus cells to grow in the presences of glycerol and 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Photoheterotrophic growth was restored by a complete fesM gene present on a replicable plasmid. A mutant fesM gene encoding a truncated FesM protein lacking the cAMP domain failed to restore the phenotype, suggesting this domain is important to the function of FesM. Measurements of reduction of P700+ and the redox state of interphotosystem electron carriers showed that cells had a slower rate of respiratory electron donation to the interphotosystem electron transport chain, and cyclic electron flow around photosystem I in fesM-D was impaired, suggesting that FesM is a critical protein for respiratory and cyclic electron flow. Phosphatase fusion analysis showed that FesM contains nine membrane-spanning helices, and all functional domains of FesM are located on the cytoplasmic face of the thylakoid membranes.




This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
W. Zhao, Q. Guo, and J. Zhao
A Membrane-Associated Mn-Superoxide Dismutase Protects the Photosynthetic Apparatus and Nitrogenase from Oxidative Damage in the Cyanobacterium Anabaena sp. PCC 7120
Plant Cell Physiol., April 1, 2007; 48(4): 563 - 572.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
D. Xu, X. Liu, C. Guo, and J. Zhao
Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002
Microbiology, July 1, 2006; 152(7): 2013 - 2021.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2005 by the American Society of Plant Biologists