Rv0802c is an acyltransferase that succinylates and acetylates mycobacterium tuberculosis nucleoid-associated protein hu

Anand, C and Santoshi, M and Singh, PR and Nagaraja, V (2021) Rv0802c is an acyltransferase that succinylates and acetylates mycobacterium tuberculosis nucleoid-associated protein hu. In: Microbiology (United Kingdom), 167 (7).

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Abstract

Among the nucleoid-associated proteins (NAPs), HU is the most conserved in eubacteria, engaged in overall chromosome organization and regulation of gene expression. Unlike other bacteria, HU from Mycobacterium tuberculosis (MtHU), has a long carboxyl terminal domain enriched in basic amino acids, resembling eukaryotic histone N-terminal tails. As with histones, MtHU undergoes post-translational modifications and we have previously identified interacting kinases, methyltransferases, an acetyltransferase and a deacetylase. Here we show that Rv0802c interacts and succinylates MtHU. Although categorized as a succinyltransferase, we show that this GNAT superfamily member can catalyse both succinylation and acetylation of MtHU with comparable kinetic parameters. Like acetylation of MtHU, succinylation of MtHU caused reduced interaction of the NAP with DNA, determined by electrophoretic mobility shift assay and surface plasmon resonance. However, in vivo expression of Rv0802c did not significantly alter the nucleoid architecture. Although such succinylation of NAPs is rare, these modifications of the archetypal NAP may provide avenues to the organism to compensate for the underrepresentation of NAPs in its genome to control the dynamics of nucleoid architecture and cellular functions. © 2021 The Authors.

Item Type:	Journal Article
Publication:	Microbiology (United Kingdom)
Publisher:	Microbiology Society
Additional Information:	The copyright for this article belongs to Microbiology Society
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	01 Dec 2021 14:41
Last Modified:	01 Dec 2021 14:41
URI:	http://eprints.iisc.ac.in/id/eprint/70027

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