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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Green KD,Biswas T,Pang AH,Willby MJ,Reed MS,Stuchlik O,Pohl J,Posey JE,Tsodikov OV,Garneau-Tsodikova Sdoi
10.1021/acs.biochem.7b01089subject
Has Abstractpub_date
2018-02-06 00:00:00pages
781-790issue
5eissn
0006-2960issn
1520-4995journal_volume
57pub_type
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