Association between intrinsic disorder and serine/threonine phosphorylation in Mycobacterium tuberculosis
- Published
- Accepted
- Subject Areas
- Biochemistry, Bioinformatics, Microbiology
- Keywords
- Protein Disorder, Intrinsic Disorder, Phosphorylation, Serine/threonine phosphorylation, Mycobacterium tuberculosis
- Copyright
- © 2014 Singh
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
- Cite this article
- 2014. Association between intrinsic disorder and serine/threonine phosphorylation in Mycobacterium tuberculosis. PeerJ PrePrints 2:e564v1 https://doi.org/10.7287/peerj.preprints.564v1
Abstract
Serine/threonine phosphorylation is an important mechanism to regulate protein function. In eukaryotes phosphorylation occurs predominantly in intrinsically disordered regions of proteins. While serine/threonine phosphorylation and protein disorder are much less prevalent in prokaryotes, M. tuberculosis has both high serine/threonine phosphorylation and disorder. Here I show that, similar to eukaryotes, serine/threonine phosphorylation sites in M. tuberculosis are highly enriched in intrinsically disordered regions, indicating similarity in substrate recognition mechanism of eukaryotic and M. tuberculosis kinases. Serine/threonine phosphorylation has been linked to the pathogenicity and survival of M. tuberculosis, thus better understanding of how its kinases recognize their substrates could have important implications in understanding and controlling the biology of this deadly pathogen.
Author Comment
This article will be submitted to PeerJ for review.