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Journal of Bacteriology, June 2009, p. 3580-3587, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.00110-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Role of the AcsF Protein in Chloroflexus aurantiacus{triangledown} ,{dagger}

Kuo-Hsiang Tang, Jianzhong Wen, Xianglu Li, and Robert E. Blankenship*

Departments of Biology and Chemistry, Campus Box 1137, Washington University, St. Louis, Missouri 63130

Received 26 January 2009/ Accepted 27 March 2009

The green phototrophic bacteria contain a unique complement of chlorophyll pigments, which self-assemble efficiently into antenna structures known as chlorosomes with little involvement of protein. The few proteins found in chlorosomes have previously been thought to have a primarily structural function. The biosynthetic pathway of the chlorosome pigments, bacteriochlorophylls c, d, and e, is not well understood. In this report, we used spectroscopic, proteomic, and gene expression approaches to investigate the chlorosome proteins of the green filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus. Surprisingly, Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase, AcsF, was identified under anaerobic growth conditions. The AcsF protein was found in the isolated chlorosome fractions, and the proteomics analysis suggested that significant portions of the AcsF proteins are not accessible to protease digestion. Additionally, quantitative real-time PCR studies showed that the transcript level of the acsF gene is not lower in anaerobic growth than in semiaerobic growth. Since the proposed enzymatic activity of AcsF requires molecular oxygen, our studies suggest that the roles of AcsF in C. aurantiacus need to be investigated further.

* Corresponding author. Mailing address: Departments of Biology and Chemistry, Campus Box 1137, Washington University, St. Louis, MO 63130. Phone: (314) 935-7971. Fax: (314) 935-4432. E-mail: blankenship{at}wustl.edu

{triangledown} Published ahead of print on 3 April 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, June 2009, p. 3580-3587, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.00110-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Li, H., Bryant, D. A. (2009). Envelope Proteins of the CsmB/CsmF and CsmC/CsmD Motif Families Influence the Size, Shape, and Composition of Chlorosomes in Chlorobaculum tepidum. J. Bacteriol. 191: 7109-7120 [Abstract] [Full Text]  


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