title: Xenopus ElrB, but not ElrA, binds RNA as an oligomer: possible role of the linker.
abstract: We have shown that ElrA and ElrB, Xenopus ELAV homologues, bind the Vg1 mRNA 3'UTR translation element in Xenopus oocytes and implicated ElrB in mediating translational repression during oogenesis. Here we report that, while ElrA and ElrB are 69% identical and both exhibit RNA binding in the nM range, recombinant ElrB, but not ElrA, is able to oligomerise. This oligomerisation is also seen with the endogenous protein. Both RNA binding and oligomerisation require the linker region flanked with two RNA recognition motifs. Our data demonstrate a novel and unique property of ElrB which may be important for its function as a translational regulator.
authors.affiliation: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
authors.forename: Agathe
authors.initials: A
authors.lastname: Devaux
authors.forename: Lucy J
authors.initials: LJ
authors.lastname: Colegrove-Otero
authors.forename: Nancy
authors.initials: N
authors.lastname: Standart
mesh_terms: D000818:Animals; D000067777:ELAV-Like Protein 2; D009865:Oocytes / Q000378:metabolism; D011485:Protein Binding; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D029867:Xenopus Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014982:Xenopus laevis
chemical_list: D000067777:ELAV-Like Protein 2; C480172:ELAVL1 protein, Xenopus; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D012261:Ribonucleoproteins; D029867:Xenopus Proteins; C000593999:elavl2 protein, Xenopus; D012313:RNA