RNA binding by Hfq and ring-forming (L)Sm proteins: a trade-off between optimal sequence readout and RNA backbone conformation.
The eukaryotic Sm and the Sm-like (LSm) proteins form a large family that includes LSm proteins in archaea and the Hfq proteins in bacteria. Commonly referred to as the (L)Sm protein family, the various members play important roles in RNA processing, decay, and riboregulation. Particularly interesting from a structural point of view is their ability to assemble into doughnut-shaped rings, which allows them to bind preferentially the uridine-rich 3'-end of RNA oligonucleotides. With an emphasis on Hfq, this review compares the RNA-binding properties of the various (L)Sm rings that were recently co-crystallized with RNA substrates, and it discusses how these properties relate to physiological function.
Department of Biochemistry; Max Planck Institute for Developmental Biology; Tübingen, Germany.
Oliver
O
Weichenrieder
D001482:Base Composition; D001665:Binding Sites; D017124:Conserved Sequence; D005786:Gene Expression Regulation; D035001:Host Factor 1 Protein / Q000737:chemistry / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D058727:RNA, Small Untranslated / Q000737:chemistry / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*
D035001:Host Factor 1 Protein; D058727:RNA, Small Untranslated; D016601:RNA-Binding Proteins; D012313:RNA
Hfq; LSm1; LSm8; RNA 3′-end recognition; RNA chaperone; RNA deadenylation; Sm; riboregulation; sRNA