Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight

Keith D. Green, Tapan Biswas, Allan H. Pang, Melisa J. Willby, Matthew S. Reed, Olga Stuchlik, Jan Pohl, James E. Posey, Oleg V. Tsodikov, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Bacterial nucleoid-associated proteins (NAPs) are critical to genome integrity and chromosome maintenance. Post-translational modifications of bacterial NAPs appear to function similarly to their better studied mammalian counterparts. The histone-like NAP HupB from Mycobacterium tuberculosis (Mtb) was previously observed to be acetylated by the acetyltransferase Eis, leading to genome reorganization. We report biochemical and structural aspects of acetylation of HupB by Eis. We also found that the SirT-family NAD+-dependent deacetylase Rv1151c from Mtb deacetylated HupB in vitro and characterized the deacetylation kinetics. We propose that activities of Eis and Rv1151c could regulate the acetylation status of HupB to remodel the mycobacterial chromosome in response to environmental changes.

Original languageEnglish
Pages (from-to)781-790
Number of pages10
JournalBiochemistry
Volume57
Issue number5
DOIs
StatePublished - Feb 6 2018

Bibliographical note

Publisher Copyright:
© 2018 American Chemical Society.

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight'. Together they form a unique fingerprint.

Cite this