Modulation of Rho-dependent transcription termination in Escherichia coli by the H-NS family of proteins

Saxena, Shivalika ; Gowrishankar, J. (2011) Modulation of Rho-dependent transcription termination in Escherichia coli by the H-NS family of proteins Journal of Bacteriology, 193 . pp. 3832-3841. ISSN 0021-9193

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Nascent transcripts in Escherichia coli that fail to be simultaneously translated are subject to a factor-dependent mechanism of termination (also termed as 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
Source:Copyright of this article belongs to American Society for Microbiology.
ID Code:93992
Deposited On:02 Jul 2012 04:45
Last Modified:02 Jul 2012 04:45

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