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 language | English |
|---|---|
| Pages (from-to) | 781-790 |
| Number of pages | 10 |
| Journal | Biochemistry |
| Volume | 57 |
| Issue number | 5 |
| DOIs | |
| State | Published - Feb 6 2018 |
Bibliographical note
Funding Information:*(O.V.T.) E-mail: oleg.tsodikov@uky.edu. *(S.G.T.) E-mail: sylviegtsodikova@uky.edu. ORCID Sylvie Garneau-Tsodikova: 0000-0002-7961-5555 Author Contributions S.G.T. and O.V.T. designed the project. K.D.G. performed all biochemical experiments. T.P., A.H.P., and O.V.T. performed the structural biology work. M.J., M.S.R., O.S., J.S., and J.E.P. conducted the mass spectrometry experiments. K.D.G., O.V.T., and S.G.T. wrote the manuscript, and all other authors provided comments. The manuscript was written through contributions of all authors. All authors have given approval to the final version of the manuscript. Funding This work was supported by a grant from the National Institutes of Health (NIH) AI090048 (to S.G.-T.). Notes The authors declare no competing financial interest.
Publisher Copyright:
© 2018 American Chemical Society.
ASJC Scopus subject areas
- Biochemistry
