4x9c
1.4A crystal structure of Hfq from Methanococcus jannaschii1.4A crystal structure of Hfq from Methanococcus jannaschii
Structural highlights
FunctionPublication Abstract from PubMedThe Sm and Sm-like proteins are widely distributed among bacteria, archaea and eukarya. They participate in many processes related to RNA-processing and regulation of gene expression. While the function of the bacterial Lsm protein Hfq and eukaryotic Sm/Lsm proteins is rather well studied, the role of Lsm proteins in Archaea is investigated poorly. In this work, the RNA-binding ability of an archaeal Hfq-like protein from Methanococcus jannaschii has been studied by X-ray crystallography, anisotropy fluorescence and surface plasmon resonance. It has been found that MjaHfq preserves the proximal RNA-binding site that usually recognizes uridine-rich sequences. Distal adenine-binding and lateral RNA-binding sites show considerable structural changes as compared to bacterial Hfq. MjaHfq did not bind mononucleotides at these sites and would not recognize single-stranded RNA as its bacterial homologues. Nevertheless, MjaHfq possesses affinity to poly(A) RNA that seems to bind at the unstructured positive-charged N-terminal tail of the protein. Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.,Nikulin A, Mikhailina A, Lekontseva N, Balobanov V, Nikonova E, Tishchenko S J Biomol Struct Dyn. 2016 Aug 1:1-14. PMID:27187760[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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