Structural analysis of sigma E interactions with core RNA polymerase and its cognate P-hsp20 promoter of Mycobacterium tuberculosis.
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| Abstract |
Alternate sigma factor plays an important role for the survival of Mycobacterium tuberculosis in adverse environmental condition. Stress-induced sigma factors are major cause for expression of genes involved in pathogenesis, dormancy and various unusual environmental conditions. In the present work, an attempt has been made to characterize one of such M. tuberculosis (Mtb) sigma factor, SigE. The structures of Mtb-SigE and Mtb-β have been predicted using comparative modelling techniques and validated. Effort has also been implied to understand the nature of interaction of SigE with the core RNA polymerase subunits which have well identified the amino acid residues in the binding interface and prompted the fact that Mtb-β' and Mtb-β interact with domain 2 and domain 4 of Mtb-SigE, respectively. Furthermore, intermolecular docking study predicted the interface between the Mtb-SigE and its putative promoter P-hsp20. The report confers the probable amino acid residues and the nitrogenous bases involved in the recognition of P-hsp20 by the sigma factor to initiate the transcription process.
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| Authors | Aayatti Mallick Gupta, Purab Pal, Sukhendu Mandal |
| Journal | Journal of biomolecular structure & dynamics (J Biomol Struct Dyn) Vol. 34 Issue 4 Pg. 792-9 ( 2016) ISSN: 1538-0254 [Electronic] England |
| PMID | 26006066 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
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