Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 35, Issue 8, Pages 1615-1628Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2016.1189849
Keywords
Lsm proteins; Hfq; archaea; RNA-protein interactions; translation regulation; crystal structure
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Funding
- Russian Scientific Foundation [14-14-00496]
- Russian Science Foundation [14-14-00496] Funding Source: Russian Science Foundation
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The 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.
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