Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/81823
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Type: Journal article
Title: The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides
Author: Standish, A.
Morona, R.
Citation: Antioxidants & Redox Signaling, 2014; 20(14):2274-2289
Publisher: Mary Ann Liebert
Issue Date: 2014
ISSN: 1557-7716
1557-7716
Statement of
Responsibility: 
Alistair James Standish and Renato Morona
Abstract: SIGNIFICANCE: Tyrosine phosphorylation and associated protein tyrosine phosphatases are gaining prominence as critical mechanisms in the regulation of fundamental processes in a wide variety of bacteria. In particular, these phosphatases have been associated with the control of the biosynthesis of capsular polysaccharides and extracellular polysaccharides, critically important virulence factors for bacteria.RECENT ADVANCES: Deletion and over-expression of the phosphatases result in altered polysaccharide biosynthesis in a range of bacteria. The recent structures of associated auto-phosphorylating tyrosine kinases has suggested that the phosphatases may be critical for the cycling of the kinases between monomers and higher order oligomers. CRITICAL ISSUES: Additional substrates of the phosphatases apart from cognate kinases are currently being identified. These are likely to be critical to our understanding of the mechanism by which polysaccharide biosynthesis is regulated. FUTURE DIRECTIONS: Ultimately, these protein tyrosine phosphatases are an attractive target for the development of novel anti-microbials. This is particularly the case for the polymerase and histidinol phosphatase family, which are predominantly found in bacteria. Furthermore, the determination of bacterial tyrosine phosphoproteomes will likely help to uncover the fundamental roles, mechanism and critical importance of these phosphatases in a wide range of bacteria.
Keywords: Bacteria; Polysaccharides; Models, Molecular; Protein Tyrosine Phosphatases
Rights: © Mary Ann Liebert
RMID: 0030000205
DOI: 10.1089/ars.2013.5726
Grant ID: http://purl.org/au-research/grants/nhmrc/565526
http://purl.org/au-research/grants/nhmrc/1048749
Appears in Collections:Molecular and Biomedical Science publications

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