title: Hfq structure, function and ligand binding.
abstract: Recent studies on Hfq have provided a deeper understanding of the multiple functions of this pleiotropic post-transcriptional regulator. Insights into the mechanism of Hfq action have come from a variety of approaches. A key finding was the characterization of two RNA binding sites: the Proximal Site, which binds sRNA and mRNA; and the Distal Site, which binds poly(A) tails. Hfq was shown to interact with PAP I, PNP and RNase E, proteins that are involved in mRNA decay and in vitro, was shown to form fibres, the physiological significance of which is unknown. Fluorescence resonance energy transfer (FRET) studies directly demonstrated the role of Hfq as a chaperone that facilitates the interaction between sRNAs and target mRNAs. There are still, however, some unresolved questions.
authors: Department of Biochemistry and Molecular Biology, Unit 1000 University of Texas MD Anderson Cancer Center, 1515 Holcombe Boulevard Houston, TX 77030-4009, USA. rgbrenna@mdanderson.org
authors: Richard G
authors: RG
authors: Brennan
authors: Todd M
authors: TM
authors: Link
mesh_terms: D001324:Autoantigens / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D035001:Host Factor 1 Protein / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D012329:RNA, Bacterial / Q000378:metabolism; D017411:Ribonucleoproteins, Small Nuclear / Q000737:chemistry / Q000378:metabolism; D055517:snRNP Core Proteins
chemical_list: D001324:Autoantigens; D029968:Escherichia coli Proteins; C087373:Hfq protein, E coli; D035001:Host Factor 1 Protein; D008024:Ligands; D012329:RNA, Bacterial; D017411:Ribonucleoproteins, Small Nuclear; D055517:snRNP Core Proteins