title: The La protein-RNA complex surfaces.
abstract: A recent issue of Molecular Cell reported that the typical nucleic acid binding surfaces of the RRM and winged-helix motifs, although present in the RNA binding protein La, are not used to engage its best-characterized ligand, 3' UUU-OH. Instead, La uses edgewise and backsides of these motifs for UUU-OH recognition, leaving open their typical surfaces for other potential interactions. These observations provide a framework for appreciating the various activities attributed to this ubiquitous nuclear phosphoprotein, which include its principal function, snRNA 3' end protection, in addition to mRNA-related and RNA chaperone-like activities, as well as DNA and chromatin-associated activity.
authors.affiliation: Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, 31 Center Drive, 2A25, Bethesda, Maryland 20892, USA. maraiar@mail.nih.gov
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Maraia
authors.forename: Mark A
authors.initials: MA
authors.lastname: Bayfield
mesh_terms: D020816:Amino Acid Motifs; D001324:Autoantigens / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D000097585:SS-B Antigen
chemical_list: D001324:Autoantigens; D046911:Macromolecular Substances; D012313:RNA; D012261:Ribonucleoproteins; D000097585:SS-B Antigen