The Structure of the Hfq Protein from Chromobacterium haemolyticum Revealed a New Variant of Regulation of RNA Binding with the Protein

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Abstract

The structure of the Hfq protein from the bacterium Chromobacterium haemolyticum, which forms crystals in two different spatial groups, has been determined. In both cases, the protein has a specific quaternary hexamer-ring structure. The obtained structure showed a previously undescribed interaction between the C-terminal unstructured part of Hfq and the amino acid residues of the proximal RNA-binding site of the protein. This contact may contribute to the regulation of the binding of RNA molecules to the Hfq protein.

About the authors

N. V. Lekontseva

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, Russia

Email: nikulin@vega.protres.ru
Россия, Пущино

A. D. Nikulin

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, Russia

Author for correspondence.
Email: nikulin@vega.protres.ru
Россия, Пущино

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