BACK TO CONTENTS   |    PDF   |    PREVIOUS   |    NEXT

Title

Implication from the predicted docked interaction of sigma H and exploration of its interaction with RNA polymerase in Mycobacterium tuberculosis

 

Authors

Aayatti Mallick Gupta1, Simanti Bhattacharya2, Angshuman Bagchi2 & Sukhendu Mandal1*

 

Affiliation

1Department of Microbiology, University of Calcutta, 35, Ballygunge Circular Road, Kolkata, 700019, India; 2Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, 741235, Nadia, India

 

Email

sukhendu1@hotmail.com; smmicrobio@caluniv.ac.in; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received February 27, 2015; Accepted March 16, 2015; Published June 30, 2015

 

Abstract

M. tuberculosis is adapted to remain active in the extreme environmental condition due to the presence of atypical sigma factors commonly called extra cytoplasmic function (ECF) sigma factors. Among the 13 sigma factors of M. tuberculosis, 10 are regarded as the ECF sigma factor that exerts their attributes in various stress response. Therefore it is of interest to describe the structural prediction of one of the ECF sigma factors, sigma H (SigH), involved in oxidative and heat stress having interaction with the β' subunit of M. tuberculosis. RNA polymerase (Mtb-RNAP). The model of Mtb-SigH was build using the commercial package of Discovery Studio version 2.5 from Accelerys (San Diego, CA, USA) containing the inbuilt MODELER module and that of β' subunit of Mtb-RNAP using Phyre Server. Further, the protein models were docked using the fully automated web tool ClusPro (cluspro.bu.edu/login.php). Mtb-SigH is a triple helical structure having a putative DNA-binding site and the β' subunit of Mtb-RNAP consists of 18-beta sheets and 22 helices. The SigH-Mtb-RNAP β' interaction studies showed that Arg26, Gln19 andAsp18, residues of SigH protein are involved in binding with Arg137, Gln140, Arg152, Asn133 and Asp144 of β' subunit of Mtb-RNAP. The predicted model helps to explore the molecular mechanism in the control of gene regulation with a novel unique target for potential new generation inhibitor.

 

Keywords

transcription, Mycobacterium sigma factor, transcription regulator, homology modelling, SigH-RNAP interaction.

 

Citation

Gupta et al.   Bioinformation 11(6): 296-301(2015)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.