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Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase

Singhal, Anshika and Arora, Gunjan and Virmani, Richa and Kundu, Parijat and Khanna, Tanya and Sajid, Andaleeb and Misra, Richa and Joshi, Jayadev and Yadav, Vikas and Samanta, Sintu and Saini, Neeru and Pandey, Amit K and Visweswariah, Sandhya S and Hentschker, Christian and Becher, Doerte and Gerth, Ulf and Singh, Yogendra (2015) Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase. In: JOURNAL OF BIOLOGICAL CHEMISTRY, 290 (43). 26218+.

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Official URL: http://dx.doi.org/10.1074/jbc.M115.687269

Abstract

Protein lysine acetylation is known to regulate multiple aspects of bacterial metabolism. However, its presence in mycobacterial signal transduction and virulence-associated proteins has not been studied. In this study, analysis of mycobacterial proteins from different cellular fractions indicated dynamic and widespread occurrence of lysine acetylation. Mycobacterium tuberculosis proteins regulating diverse physiological processes were then selected and expressed in the surrogate host Mycobacterium smegmatis. The purified proteins were analyzed for the presence of lysine acetylation, leading to the identification of 24 acetylated proteins. In addition, novel lysine succinylation and propionylation events were found to co-occur with acetylation on several proteins. Protein-tyrosine phosphatase B (PtpB), a secretory phosphatase that regulates phosphorylation of host proteins and plays a critical role in Mycobacterium infection, is modified by acetylation and succinylation at Lys-224. This residue is situated in a lid region that covers the enzyme's active site. Consequently, acetylation and succinylation negatively regulate the activity of PtpB.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics
Depositing User: Id for Latest eprints
Date Deposited: 24 Nov 2015 06:02
Last Modified: 24 Nov 2015 06:02
URI: http://eprints.iisc.ac.in/id/eprint/52816

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