ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

The fused SnoaL_2 domain in the Mycobacterium tuberculosis sigma factor sigma(J) modulates promoter recognition

Goutam, Kapil and Gupta, Arvind K and Gopal, Balasubramanian (2017) The fused SnoaL_2 domain in the Mycobacterium tuberculosis sigma factor sigma(J) modulates promoter recognition. In: NUCLEIC ACIDS RESEARCH, 45 (16). pp. 9760-9772.

[img] PDF
Nuc_Aci_Res_45-16_9760_2017.pdf - Published Version
Restricted to Registered users only

Download (4MB) | Request a copy
Official URL: http://doi.org/10.1093/nar/gkx609


Extra-cytoplasmic function (ECF) sigma-factors are widespread in bacteria, linking environmental stimuli with changes in gene expression. These transcription factors span several phylogenetically distinct groups and are remarkably diverse in their activation and regulatory mechanisms. Here, we describe the structural and biochemical features of a Mycobacterium tuberculosis ECF factor sigma(J) that suggests that the SnoaL2 domain at the C-terminus can modulate the activity of this initiation factor in the absence of a cognate regulatory anti-sigma factor. M. tu-berculosis sigma(J) can bind promoter DNA in vitro; this interaction is substantially impaired by the removal of the SnoaL2 domain. This finding is consistent with assays to evaluate sigma(J)-mediated gene expression. Structural similarity of the SnoaL2 domain with epoxide hydrolases also suggests a novel functional role for this domain. The conserved sequence features between M. tuberculosis sigma(J) and other members of the ECF41 family of sigma-factors suggest that the regulatory mechanism involving the C-terminal SnoaL2 domain is likely to be retained in this family of proteins. These studies suggest that the ECF41 family of sigma-factors incorporate features of both-the sigma(70) family and bacterial one-component systems thereby providing a direct mechanism to implement environment-mediated transcription changes.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the OXFORD UNIV PRESS, GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 13 Oct 2017 04:53
Last Modified: 13 Oct 2017 04:53
URI: http://eprints.iisc.ac.in/id/eprint/58014

Actions (login required)

View Item View Item