Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight
| Autor: | Keith D. Green, Sylvie Garneau-Tsodikova, Tapan Biswas, Jan Pohl, Allan H. Pang, Oleg V. Tsodikov, Melisa J. Willby, James E. Posey, Olga Stuchlik, Matthew S. Reed |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation 030106 microbiology Crystallography X-Ray Biochemistry Article Histone Deacetylases Bacterial genetics Histones Mycobacterium tuberculosis 03 medical and health sciences Bacterial Proteins Acetyltransferases Tandem Mass Spectrometry Drug Resistance Multiple Bacterial Protein Interaction Mapping Transferase Amino Acid Sequence Cloning Molecular Regulation of gene expression Sequence Homology Amino Acid biology Chemistry Lysine Acetylation Gene Expression Regulation Bacterial biology.organism_classification Peptide Fragments Recombinant Proteins Kinetics Histone Acetyltransferase biology.protein NAD+ kinase Protein Processing Post-Translational Sequence Alignment |
| Zdroj: | Biochemistry. 57:781-790 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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