{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stanek KA"],"funding":["NCRR NIH HHS","Thomas F. and Kate Miller Jeffress Memorial Trust","NIGMS NIH HHS","National Science Foundation, Division of Molecular and Cellular Biosciences"],"pagination":["294-315"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5379935"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["73(Pt 4)"],"pubmed_abstract":["The host factor Hfq, as the bacterial branch of the Sm family, is an RNA-binding protein involved in the post-transcriptional regulation of mRNA expression and turnover. Hfq facilitates pairing between small regulatory RNAs (sRNAs) and their corresponding mRNA targets by binding both RNAs and bringing them into close proximity. Hfq homologs self-assemble into homo-hexameric rings with at least two distinct surfaces that bind RNA. Recently, another binding site, dubbed the `lateral rim', has been implicated in sRNA·mRNA annealing; the RNA-binding properties of this site appear to be rather subtle, and its degree of evolutionary conservation is unknown. An Hfq homolog has been identified in the phylogenetically deep-branching thermophile Aquifex aeolicus (Aae), but little is known about the "],"journal":["Acta crystallographica. Section D, Structural biology"],"pubmed_title":["Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode."],"pmcid":["PMC5379935"],"funding_grant_id":["1350957","T32 GM008136","J-971","S10 RR029205","T32 GM080186","P41 GM103403"],"pubmed_authors":["Patterson-West J","Mura C","Randolph PS","Stanek KA"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode.","description":"The host factor Hfq, as the bacterial branch of the Sm family, is an RNA-binding protein involved in the post-transcriptional regulation of mRNA expression and turnover. Hfq facilitates pairing between small regulatory RNAs (sRNAs) and their corresponding mRNA targets by binding both RNAs and bringing them into close proximity. Hfq homologs self-assemble into homo-hexameric rings with at least two distinct surfaces that bind RNA. Recently, another binding site, dubbed the `lateral rim', has been implicated in sRNA·mRNA annealing; the RNA-binding properties of this site appear to be rather subtle, and its degree of evolutionary conservation is unknown. An Hfq homolog has been identified in the phylogenetically deep-branching thermophile Aquifex aeolicus (Aae), but little is known about the ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Apr","modification":"2026-05-30T13:57:46.006Z","creation":"2019-03-27T02:40:23Z"},"accession":"S-EPMC5379935","cross_references":{"pubmed":["28375142"],"doi":["10.1107/S2059798317000031"]}}