Scientific article

Structure of an Escherichia coli Hfq:RNA complex at 0.97 Å resolution

Publication date2014-10-31
First online date2014-10-31

In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA–mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq–RNA interaction in exceptional detail.

  • Escherichia coli
  • Hfq
  • RNA chaperones
Affiliation Not a UNIGE publication
Citation (ISO format)
SCHULZ, Eike C., BARABAS, Orsolya. Structure of an <i>Escherichia coli</i> Hfq:RNA complex at 0.97 Å resolution. In: Acta crystallographica. Section F, Structural biology communications, 2014, vol. 70, n° 11, p. 1492–1497. doi: 10.1107/S2053230X14020044
Main files (1)
Article (Published version)
ISSN of the journal2053-230X

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