[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Saxena, S. and Gowrishankar, J. (2011) Modulation of Rho-Dependent Transcription Termination in Escherichia coli by the H-NS Family of Proteins. Journal of Bacteriology, 193 (15). pp. 3832-3841. ISSN 0021-9193

[img]
Preview
Text
J Bacteriol 193 p3832.pdf

Download (1136Kb) | Preview

Abstract

Nascent transcripts in Escherichia coli that fail to be simultaneously translated are subject to a factor-dependent mechanism of termination (also termed a polarity) that involves the proteins Rho and NusG. In this study, we found that overexpression of YdgT suppressed the polarity relief phenotypes and restored the efficiency of termination in rho or nusG mutants. YdgT and Hha belong to the H-NS and StpA family of proteins that repress a large number of genes in Gram-negative bacteria. Variants of H-NS defective in one or the other of its two dimerization domains, but not those defective in DNA binding alone, also conferred a similar suppression phenotype in rho and nusG mutants. YdgT overexpression was associated with derepression of proU, a prototypical H-NS-silenced locus. Polarity relief conferred by rho or nusG was unaffected in a derivative completely deficient for both H-NS and StpA, although the suppression effects of YdgT or the oligomerization-defective H-NS variants were abolished in this background. Transcription elongation rates in vivo were unaffected in any of the suppressor-bearing strains. Finally, the polarity defects of rho and nusG mutants were exacerbated by Hha and YdgT deficiency. A model is proposed that invokes a novel role for the polymeric architectural scaffold formed on DNA by H-NS and StpA independent of the gene-silencing functions of these nucleoid proteins, in modulating Rho-dependent transcription termination such that interruption of the scaffold (as obtained by expression either of the H-NS oligomerization variants or of YdgT) is associated with improved termination efficiency in the rho and nusG mutants.

Item Type: Article
Depositing User: Dr P Divakar
Date Deposited: 03 Sep 2015 07:21
Last Modified: 03 Sep 2015 07:21
URI: http://cdfd.sciencecentral.in/id/eprint/460

Actions (login required)

View Item View Item