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cAMP-regulated Protein Lysine Acetylases in Mycobacteria

Nambi, Subhalaxmi and Basu, Nirmalya and Visweswariah, Sandhya S (2010) cAMP-regulated Protein Lysine Acetylases in Mycobacteria. In: Journal of Biological Chemistry, 285 (32). pp. 24313-24323.

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Official URL: http://www.jbc.org/content/285/32/24313.short


Cyclic AMP synthesized by Mycobacterium tuberculosis has been shown to play a role in pathogenesis. However, the high levels of intracellularcAMP found in both pathogenic and nonpathogenic mycobacteria suggest that additional and important biological processes are regulated by characterization of novel cAMP-binding proteins in M. smegmatis and M. tuberculosis (MSMEG_5458 and Rv0998, respectively) that contain a cyclic nucleotide binding domain fused to a domain that shows similarity to the GNAT family of acetyltransferases. We detect protein lysine acetylation in mycobacteria and identify a universal stress protein (USP) as a substrate of MSMEG_5458. Acetylation of a lysine residue in USP is regulated by cAMP, and using a strain deleted for MSMEG_5458, we show that USP is indeed an in vivo substrate for MSMEG_5458. The Rv0998 protein shows a strict cAMP-dependent acetylation of USP, despite a lower affinity for cAMP than MSMEG_5458. Thus, this report not only represents the first demonstration of protein lysine acetylation in mycobacteria but also describes a unique functional interplay between a cyclic nucleotide binding domain and a protein acetyltransferase.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics
Depositing User: Id for Latest eprints
Date Deposited: 23 Aug 2010 10:55
Last Modified: 19 Sep 2010 06:14
URI: http://eprints.iisc.ac.in/id/eprint/31492

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