Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M606360200 on August 21, 2006

J. Biol. Chem., Vol. 281, Issue 43, 32705-32713, October 27, 2006
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
281/43/32705    most recent
M606360200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Promnares, K.
Right arrow Articles by Tichy, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Promnares, K.
Right arrow Articles by Tichy, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Cyanobacterial Small Chlorophyll-binding Protein ScpD (HliB) Is Located on the Periphery of Photosystem II in the Vicinity of PsbH and CP47 Subunits*

Kamoltip Promnares{ddagger}§, Josef Komenda§, Ladislav Bumba||**, Jana Nebesarova||, Frantisek Vacha{ddagger}§||, and Martin Tichy§1

From the {ddagger}Faculty of Biological Sciences, University of South Bohemia, 370 05 Ceske Budejovice, Czech Republic, the §Institute of Physical Biology, University of South Bohemia, 373 33 Nové Hrady, Czech Republic, the Laboratory of Photosynthesis, Institute of Microbiology, Czech Academy of Sciences, 379 81 Trebon, Czech Republic, the ||Biological Center, Czech Academy of Sciences, 370 05 Ceske Budejovice, Czech Republic, and the **Institute of Microbiology, Czech Academy of Sciences, 142 20 Prague, Czech Republic

Cyanobacteria contain several genes coding for small one-helix proteins called SCPs or HLIPs with significant sequence similarity to chlorophyll a/b-binding proteins. To localize one of these proteins, ScpD, in the cells of the cyanobacterium Synechocystis sp. PCC 6803, we constructed several mutants in which ScpD was expressed as a His-tagged protein (ScpDHis). Using two-dimensional native-SDS electrophoresis of thylakoid membranes or isolated Photosystem II (PSII), we determined that after high-light treatment most of the ScpDHis protein in a cell is associated with PSII. The ScpDHis protein was present in both monomeric and dimeric PSII core complexes and also in the core subcomplex lacking CP43. However, the association with PSII was abolished in the mutant lacking the PSII subunit PsbH. In a PSII mutant lacking cytochrome b559, which does not accumulate PSII, ScpDHis is associated with CP47. The interaction of ScpDHis with PsbH and CP47 was further confirmed by electron microscopy of PSII labeled with Ni-NTA Nanogold. Single particle image analysis identified the location of the labeled ScpDHis at the periphery of the PSII core complex in the vicinity of the PsbH and CP47. Because of the fact that ScpDHis did not form any large structures bound to PSII and because of its accumulation in PSII subcomplexes containing CP47 and PsbH we suggest that ScpD is involved in a process of PSII assembly/repair during the turnover of pigment-binding proteins, particularly CP47.


Received for publication, July 5, 2006 , and in revised form, August 18, 2006.

* The work was supported in part by the project MSM6007665808 of the Ministry of Education, Youth and Sports of the Czech Republic, and by the Czech Academy of Sciences Institutional Research Concepts AV0Z50200510 and AV0Z50510513. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 To whom correspondence should be addressed: Inst. of Microbiology, Laboratory of Photosynthesis, Opatovicky mlyn, 379 81 Trebon, Czech Republic. Tel.: 420-384-722-268; Fax: 420-384-721-246; E-mail: tichym{at}alga.cz.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Plant Physiol.Home page
M. Dobakova, R. Sobotka, M. Tichy, and J. Komenda
Psb28 Protein Is Involved in the Biogenesis of the Photosystem II Inner Antenna CP47 (PsbB) in the Cyanobacterium Synechocystis sp. PCC 6803
Plant Physiology, February 1, 2009; 149(2): 1076 - 1086.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
Q. Wang, S. Jantaro, B. Lu, W. Majeed, M. Bailey, and Q. He
The High Light-Inducible Polypeptides Stabilize Trimeric Photosystem I Complex under High Light Conditions in Synechocystis PCC 6803
Plant Physiology, July 1, 2008; 147(3): 1239 - 1250.
[Abstract] [Full Text] [PDF]


Home page
Mol PlantHome page
O. Kilian, A. S. Steunou, A. R. Grossman, and D. Bhaya
A Novel Two Domain-Fusion Protein in Cyanobacteria with Similarity to the CAB/ELIP/HLIP Superfamily: Evolutionary Implications and Regulation
Mol Plant, January 1, 2008; 1(1): 155 - 166.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Vavilin, D. Yao, and W. Vermaas
Small Cab-like Proteins Retard Degradation of Photosystem II-associated Chlorophyll in Synechocystis sp. PCC 6803: KINETIC ANALYSIS OF PIGMENT LABELING WITH 15N AND 13C
J. Biol. Chem., December 28, 2007; 282(52): 37660 - 37668.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement