NDLI: Systematic Analysis of Mycobacterial Acylation Reveals First Example of Acylation-mediated Regulation of Enzyme Activity of a Bacterial Phosphatase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Khanna, Tanya Samanta, Sintu Joshi, Jayadev Yadav, Vikas Pandey, Amit K. Hentschker, Christian Arora, Gunjan Misra, Richa Saini, Neeru Becher, Dörte Singhal, Anshika Virmani, Richa Gerth, Ulf Kundu, Parijat Visweswariah, Sandhya S. Sajid, Andaleeb Singh, Yogendra
Description	Author Affiliation: Singhal A ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Arora G ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India, the Translational Health Science and Technology Institute, Faridabad 121001, India.); Virmani R ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Kundu P ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Khanna T ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Sajid A ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Misra R ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Joshi J ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Yadav V ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Samanta S ( the Indian Institute of Science, Bangalore 560012, India, and.); Saini N ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India.); Pandey AK ( the Translational Health Science and Technology Institute, Faridabad 121001, India, amitpandey@thsti.res.in.); Visweswariah SS ( the Indian Institute of Science, Bangalore 560012, India, and.); Hentschker C ( the Institute of Microbiology, Ernst-Moritz-Arndt-University Greifswald, D-17487 Greifswald, Germany.); Becher D ( the Institute of Microbiology, Ernst-Moritz-Arndt-University Greifswald, D-17487 Greifswald, Germany.); Gerth U ( the Institute of Microbiology, Ernst-Moritz-Arndt-University Greifswald, D-17487 Greifswald, Germany ulf.gerth@uni-greifswald.de.); Singh Y ( From the CSIR-Institute of Genomics and Integrative Biology, Delhi 110007, India, ysingh@igib.res.in.)
Abstract	Protein lysine acetylation is known to regulate multiple aspects of bacterial metabolism. However, its presence in mycobacterial signal transduction and virulence-associated proteins has not been studied. In this study, analysis of mycobacterial proteins from different cellular fractions indicated dynamic and widespread occurrence of lysine acetylation. Mycobacterium tuberculosis proteins regulating diverse physiological processes were then selected and expressed in the surrogate host Mycobacterium smegmatis. The purified proteins were analyzed for the presence of lysine acetylation, leading to the identification of 24 acetylated proteins. In addition, novel lysine succinylation and propionylation events were found to co-occur with acetylation on several proteins. Protein-tyrosine phosphatase B (PtpB), a secretory phosphatase that regulates phosphorylation of host proteins and plays a critical role in Mycobacterium infection, is modified by acetylation and succinylation at Lys-224. This residue is situated in a lid region that covers the enzyme's active site. Consequently, acetylation and succinylation negatively regulate the activity of PtpB.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	43
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-10-23
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Mycobacterium Tuberculosis Metabolism Phosphoric Monoester Hydrolases Acylation Amino Acid Sequence Molecular Sequence Data Enzymology Chemistry Phosphorylation Protein Conformation Sequence Homology, Amino Acid Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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