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C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation.

Publication ,  Journal Article
Olsen, AS; Møller-Jensen, J; Brennan, RG; Valentin-Hansen, P
Published in: J Mol Biol
November 26, 2010

The prokaryotic Sm-like protein Hfq plays an essential role in the stability and function of trans-encoded small regulatory RNAs in enterobacteria that function in posttranscriptional control by base-pairing with cognate target mRNAs. Hfq associates with both regulatory RNA and target RNA, and its interaction promotes annealing. So far, mutational and structural studies have established that Escherichia coli Hfq contains two separate RNA binding sites that are part of the conserved N-terminal portion of the protein. Moreover, it has been suggested that the nonconserved C-terminal extension of E. coli Hfq might constitute a third RNA interaction surface with specificity for mRNA. However, the role of the C-terminus has not been fully resolved but is clearly important for a complete understanding of Hfq function in posttranscriptional regulation and RNA decay. Here we examined the ability of E. coli Hfq derivatives, consisting of the conserved core and short C-terminal extensions, to support the regulation of rpoS expression and riboregulation by various well-characterized small regulatory RNAs. Our data show that, in all cases tested, the truncated proteins are fully capable of promoting posttranscriptional control, indicating that the C-terminal tail of E. coli Hfq plays a small role or no role in riboregulation.

Duke Scholars

Published In

J Mol Biol

DOI

EISSN

1089-8638

Publication Date

November 26, 2010

Volume

404

Issue

2

Start / End Page

173 / 182

Location

Netherlands

Related Subject Headings

  • Sigma Factor
  • Recombinant Proteins
  • RNA, Messenger
  • RNA, Bacterial
  • RNA Processing, Post-Transcriptional
  • Protein Structure, Secondary
  • Protein Conformation
  • Peptide Fragments
  • Molecular Sequence Data
  • Models, Molecular
 

Citation

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Olsen, A. S., Møller-Jensen, J., Brennan, R. G., & Valentin-Hansen, P. (2010). C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation. J Mol Biol, 404(2), 173–182. https://doi.org/10.1016/j.jmb.2010.09.038
Olsen, Anders Steno, Jakob Møller-Jensen, Richard G. Brennan, and Poul Valentin-Hansen. “C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation.J Mol Biol 404, no. 2 (November 26, 2010): 173–82. https://doi.org/10.1016/j.jmb.2010.09.038.
Olsen AS, Møller-Jensen J, Brennan RG, Valentin-Hansen P. C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation. J Mol Biol. 2010 Nov 26;404(2):173–82.
Olsen, Anders Steno, et al. “C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation.J Mol Biol, vol. 404, no. 2, Nov. 2010, pp. 173–82. Pubmed, doi:10.1016/j.jmb.2010.09.038.
Olsen AS, Møller-Jensen J, Brennan RG, Valentin-Hansen P. C-terminally truncated derivatives of Escherichia coli Hfq are proficient in riboregulation. J Mol Biol. 2010 Nov 26;404(2):173–182.
Journal cover image

Published In

J Mol Biol

DOI

EISSN

1089-8638

Publication Date

November 26, 2010

Volume

404

Issue

2

Start / End Page

173 / 182

Location

Netherlands

Related Subject Headings

  • Sigma Factor
  • Recombinant Proteins
  • RNA, Messenger
  • RNA, Bacterial
  • RNA Processing, Post-Transcriptional
  • Protein Structure, Secondary
  • Protein Conformation
  • Peptide Fragments
  • Molecular Sequence Data
  • Models, Molecular