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Photosynthesis Research

, Volume 110, Issue 3, pp 153–168 | Cite as

Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of cells grown chemoheterotrophically and photoheterotrophically

  • Li Cao
  • Donald A. Bryant
  • Athena A. Schepmoes
  • Kajetan Vogl
  • Richard D. Smith
  • Mary S. Lipton
  • Stephen J. Callister
Regular Paper

Abstract

Chloroflexus aurantiacus J-10-fl is a thermophilic green bacterium, a filamentous anoxygenic phototroph, and the model organism of the phylum Chloroflexi. We applied high-throughput, liquid chromatography–mass spectrometry in a global quantitative proteomics investigation of C. aurantiacus cells grown under oxic (chemoorganoheterotrophically) and anoxic (photoorganoheterotrophically) redox states. Our global analysis identified 13,524 high-confidence peptides that matched to 1,286 annotated proteins, 242 of which were either uniquely identified or significantly increased in abundance under photoheterotrophic culture condition. Fifty-four of the 242 proteins are previously characterized photosynthesis-related proteins, including chlorosome proteins, proteins involved in the bacteriochlorophyll biosynthesis, 3-hydroxypropionate (3-OHP) CO2 fixation pathway, and components of electron transport chains. The remaining 188 proteins have not previously been reported. Of these, five proteins were found to be encoded by genes from a novel operon and observed only in photoheterotrophically grown cells. These proteins candidates may prove useful in further deciphering the phototrophic physiology of C. aurantiacus and other filamentous anoxygenic phototrophs.

Keywords

Chloroflexus aurantiacus J-10-fl Comparative proteomics Photosynthesis Liquid chromatography–mass spectrometry 

Abbreviations

FAP

Filamentous anoxygenic phototrophic

3-OHP

3-Hydroxypropionate

BChl

Bacteriochlorophyll

ACIII

Alternative complex III

LC–MS

Liquid chromatography–mass spectrometry

HPLC

High pressure liquid chromatography

COG

Clusters of orthologous groups

Notes

Acknowledgments

The research described in this article was funded by the Genomic Science Program sponsored by the U. S. Department of Energy Office of Biological and Environmental Research (DOE/BER) and performed in the Environmental Molecular Sciences Laboratory, a DOE/BER national scientific user facility located at Pacific Northwest National Laboratory (PNNL) in Richland, Washington. PNNL is a multi-program national laboratory operated by Battelle for the DOE under Contract DE-ACO5-76RLO 1830. D. A. B. additionally acknowledges support from DOE Office of Basic Energy Sciences (DE-FG02-94ER20137). The authors wish to acknowledge Dr. Yusuke Tsukatani for helpful discussion. Mass spectrometry data used in this study can be requested at http://omics.pnl.gov.

Supplementary material

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Supplementary material 1 (DOC 1548 kb)
11120_2011_9711_MOESM2_ESM.xlsx (137 kb)
Supplementary material 2 (XLSX 136 kb)
11120_2011_9711_MOESM3_ESM.xlsx (26 kb)
Supplementary material 3 (XLSX 25 kb)

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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Li Cao
    • 1
  • Donald A. Bryant
    • 2
  • Athena A. Schepmoes
    • 1
  • Kajetan Vogl
    • 2
  • Richard D. Smith
    • 1
  • Mary S. Lipton
    • 1
  • Stephen J. Callister
    • 1
  1. 1.Biological Separations and Mass SpectrometryPacific Northwest National LaboratoryRichlandUSA
  2. 2.Department of Biochemistry and Molecular BiologyThe Pennsylvania State UniversityUniversity ParkUSA

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