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J Proteomics. 2014 Jan 31;97:265-86. doi: 10.1016/j.jprot.2013.08.012. Epub 2013 Aug 28.

Beyond gene expression: the impact of protein post-translational modifications in bacteria.

Author information

1
School of Molecular Bioscience, School of Medical Sciences, The University of Sydney, 2006, Australia.
2
School of Molecular Bioscience, School of Medical Sciences, The University of Sydney, 2006, Australia; Discipline of Pathology, School of Medical Sciences, The University of Sydney, 2006, Australia. Electronic address: stuart.cordwell@sydney.edu.au.

Abstract

The post-translational modification (PTM) of proteins plays a critical role in the regulation of a broad range of cellular processes in eukaryotes. Yet their role in governing similar systems in the conventionally presumed 'simpler' forms of life has been largely neglected and, until recently, was thought to occur only rarely, with some modifications assumed to be limited to higher organisms alone. Recent developments in mass spectrometry-based proteomics have provided an unparalleled power to enrich, identify and quantify peptides with PTMs. Additional modifications to biological molecules such as lipids and carbohydrates that are essential for bacterial pathophysiology have only recently been detected on proteins. Here we review bacterial protein PTMs, focusing on phosphorylation, acetylation, proteolytic degradation, methylation and lipidation and the roles they play in bacterial adaptation - thus highlighting the importance of proteomic techniques in a field that is only just in its infancy. This article is part of a Special Issue entitled: Trends in Microbial Proteomics.

KEYWORDS:

ADP-ribosyltransferase; ART; AcK; AcS; Bacterial signalling; CID; GCN5-like protein N-acetyltransferase; GNAT; HCD; LMW; Lnt; Lol; MCP; Mass spectrometry; N-acetyltransferase; NAT; PTM; Peptide enrichment; Post-translational modifications; Pup; TCR; acetyl-coA synthetase; apolipoprotein transacylase; collision-induced dissociation; higher collisional dissociation; localisation of lipoproteins; low molecular weight; lysine acetylation; methyl-accepting chemotaxis protein; pCh; pEtN; phosphocholine; phosphoethanolamine; post-translational modification; protein ubiquitin-like protein; two-component regulation

PMID:
23994099
DOI:
10.1016/j.jprot.2013.08.012
[Indexed for MEDLINE]

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