Label-free LC–MS/MS identification of phosphatidylglycerol-regulated proteins in Synechocystis sp. PCC6803

Authors

  • Tatjana Talamantes,

    Corresponding author
    1. Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, TX, USA
    Current affiliation:
    1. Tatjana Talamantes, Thermo Fisher Scientific, Training Institute, 1400 Northpoint Parkway, West Palm Beach, FL, USA
    • Correspondence: Professor Laszlo Prokai, Department of Pharmacology and Neuroscience, University of North Texas Health Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107-2699, USA

      E-mail: Laszlo.Prokai@unthsc.edu

      Fax: +1-817-735-2118

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  • Bettina Ughy,

    1. Biological Research Centre of the Hungarian Academy of Sciences, Institute of Plant Biology, Szeged, Hungary
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  • Ildikó Domonkos,

    1. Biological Research Centre of the Hungarian Academy of Sciences, Institute of Plant Biology, Szeged, Hungary
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  • Mihály Kis,

    1. Biological Research Centre of the Hungarian Academy of Sciences, Institute of Plant Biology, Szeged, Hungary
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  • Zoltán Gombos,

    1. Biological Research Centre of the Hungarian Academy of Sciences, Institute of Plant Biology, Szeged, Hungary
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  • Laszlo Prokai

    Corresponding author
    1. Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, TX, USA
    • Correspondence: Professor Laszlo Prokai, Department of Pharmacology and Neuroscience, University of North Texas Health Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107-2699, USA

      E-mail: Laszlo.Prokai@unthsc.edu

      Fax: +1-817-735-2118

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Abstract

We present a proteomics dataset combining SDS-PAGE prefractionation and data-dependent LC–MS/MS that enables the identification of phosphatidylglycerol-regulated proteins in the pgsA mutant of Synechocystis sp. PCC6803, a cyanobacterium strain that grows with this indispensable phospholipid added exogenously. We searched the acquired raw data against a composite protein sequence database of Synechocystis using MASCOT, and employed Progenesis LC-MS software for label-free quantification based on extracted peptide intensities to detect changes in protein abundances upon phospholipid withdrawal. Protein identifications were validated using rigorous criteria, and our analysis of the dataset revealed 80 phosphatidylglycerol-regulated proteins involved in various cellular processes including photosynthesis, respiration, metabolism, transport, transcription, and translation. The data have been deposited to the ProteomeXchange with identifier PXD000363 (http://proteomecentral.proteomexchange.org/dataset/PXD000363).

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