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

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 e...

Full description

Saved in:
Bibliographic Details
Published in:Proteomics (Weinheim) 2014-05, Vol.14 (9), p.1053-1057
Main Authors: Talamantes, Tatjana, Ughy, Bettina, Domonkos, Ildikó, Kis, Mihály, Gombos, Zoltán, Prokai, Laszlo
Format: Article
Language:English
Subjects:
Bacterial Proteins - analysis
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bioinformatics
Chromatography, Liquid - methods
Cyanobacteria
GeLC-MS/MS
Phosphatidylglycerol
Phosphatidylglycerols - metabolism
Proteins
Proteome - analysis
Proteome - chemistry
Proteome - metabolism
Proteomics - methods
Quantitative label-free proteomics
Synechocystis
Synechocystis - chemistry
Synechocystis - metabolism
Tandem Mass Spectrometry - methods
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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).
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.201300372