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Journal of Bacteriology, October 2007, p. 7464-7474, Vol. 189, No. 20
0021-9193/07/$08.00+0     doi:10.1128/JB.00946-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Proteomic Characterization of the Rhodobacter sphaeroides 2.4.1 Photosynthetic Membrane: Identification of New Proteins{triangledown} ,{dagger}

Xiaohua Zeng,1 Jung Hyeob Roh,1 Stephen J. Callister,2 Christine L. Tavano,3 Timothy J. Donohue,3 Mary S. Lipton,2 and Samuel Kaplan1*

Department of Microbiology and Molecular Genetics, University of Texas Health Science Center, Houston, Texas 77030,1 Biological Separations and Mass Spectrometry, Pacific Northwest National Laboratory, Richland, Washington 99352,2 Department of Bacteriology, University of Wisconsin—Madison, Madison, Wisconsin 537063

Received 14 June 2007/ Accepted 8 August 2007

The Rhodobacter sphaeroides intracytoplasmic membrane (ICM) is an inducible membrane that is dedicated to the major events of bacterial photosynthesis, including harvesting light energy, separating primary charges, and transporting electrons. In this study, multichromatographic methods coupled with Fourier transform ion cyclotron resonance mass spectrometry, combined with subcellular fractionation, was used to test the hypothesis that the photosynthetic membrane of R. sphaeroides 2.4.1 contains a significant number of heretofore unidentified proteins in addition to the integral membrane pigment-protein complexes, including light-harvesting complexes 1 and 2, the photochemical reaction center, and the cytochrome bc1 complex described previously. Purified ICM vesicles are shown to be enriched in several abundant, newly identified membrane proteins, including a protein of unknown function (AffyChip designation RSP1760) and a possible alkane hydroxylase (RSP1467). When the genes encoding these proteins are mutated, specific photosynthetic phenotypes are noted, illustrating the potential new insights into solar energy utilization to be gained by this proteomic blueprint of the ICM. In addition, proteins necessary for other cellular functions, such as ATP synthesis, respiration, solute transport, protein translocation, and other physiological processes, were also identified to be in association with the ICM. This study is the first to provide a more global view of the protein composition of a photosynthetic membrane from any source. This protein blueprint also provides insights into potential mechanisms for the assembly of the pigment-protein complexes of the photosynthetic apparatus, the formation of the lipid bilayer that houses these integral membrane proteins, and the possible functional interactions of ICM proteins with activities that reside in domains outside this specialized bioenergetic membrane.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, University of Texas Health Science Center, Houston TX, 77030. Phone: (713) 500-5502. Fax: (713) 500-5499. E-mail: Samuel.Kaplan{at}uth.tmc.edu

{triangledown} Published ahead of print on 17 August 2007.

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

Journal of Bacteriology, October 2007, p. 7464-7474, Vol. 189, No. 20
0021-9193/07/$08.00+0     doi:10.1128/JB.00946-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Eraso, J. M., Kaplan, S. (2009). Regulation of Gene Expression by PrrA in Rhodobacter sphaeroides 2.4.1: Role of Polyamines and DNA Topology. J. Bacteriol. 191: 4341-4352 [Abstract] [Full Text]  
  • Bruscella, P., Eraso, J. M., Roh, J. H., Kaplan, S. (2008). The Use of Chromatin Immunoprecipitation to Define PpsR Binding Activity in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 190: 6817-6828 [Abstract] [Full Text]  
  • Eraso, J. M., Roh, J. H., Zeng, X., Callister, S. J., Lipton, M. S., Kaplan, S. (2008). Role of the Global Transcriptional Regulator PrrA in Rhodobacter sphaeroides 2.4.1: Combined Transcriptome and Proteome Analysis. J. Bacteriol. 190: 4831-4848 [Abstract] [Full Text]  


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