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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/1520
Title: In silico and proteomic analysis of protein methyltransferase CheR from Bacillus subtilis
Authors: Batra M.
Sharma R.
Chandra V.
Aggarwal M.
Agarwal U.
Gupta P.
Singh, Rajesh Pratap
Tomar, Shailly
Published in: International Journal of Biological Macromolecules
Abstract: Protein methyltransferase (CheR) catalyzes the methylation of the cytosolic domain of the membrane bound chemotaxis receptors, and plays a pivotal role in the chemotactic signal transduction pathway in bacteria. Crystal structure of CheR is available only from the gram-negative bacterium Salmonella typhimurium (. StCheR), which contain a catalytic C-terminal domain, encompassing a ?-subdomain, connected via a linker to the N-terminal domain. The structural-functional similitude between CheR of the gram-negative and the gram-positive bacteria remains obscure. We investigated CheR, from a gram-positive bacterium, Bacillus subtilis (. BsCheR), and have identified the functional roles of its N-terminal domain, by using the in silico molecular modeling and docking approach along with mass spectrophotometry and sequence analysis. The structural studies established that the N-terminal domain directly bound to S-Adenosyl-. l-homocysteine (SAH). Structural and sequence analyses revealed that the ?2 helix of the N-terminal domain was involved in the recognition of the methylation site of the chemotactic receptor. Additionally, immunoblot analysis showed that the purified BsCheR was phosphorylated. Further, mass spectrometry studies detected the phosphorylation at Thr3 position in the N-terminal domain of BsCheR. Phosphorylation of BsCheR suggested a regulatory role of the N-terminal domain, analogous to its antagonistic enzyme, the chemotaxis-specific methylesterase (CheB). © 2015 Elsevier B.V.
Citation: International Journal of Biological Macromolecules(2015), 77(): 168-180
URI: https://doi.org/10.1007/s11418-015-0904-x
http://repository.iitr.ac.in/handle/123456789/1520
Issue Date: 2015
Publisher: Elsevier B.V.
Keywords: Chemotaxis
CheR
Methyltransferase
ISSN: 1418130
Author Scopus IDs: 57188933381
57209347974
36131012800
54411866100
57188924753
57205675549
57208931324
57203506001
Author Affiliations: Batra, M., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Sharma, R., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Chandra, V., Council of Scientific and Indus
Funding Details: The authors thank Macromolecular Crystallographic Unit (MCU), IIC, and IIT, Roorkee for providing protein purification and computational facilities; IMTech-CSIR for providing Mass Spectrometry and proteomics facilities. MB acknowledges the University Gran
Corresponding Author: Tomar, S.; Department of Biotechnology, Indian Institute of Technology RoorkeeIndia; email: shailfbt@iitr.ac.in
Appears in Collections:Journal Publications [BT]

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