title: Tethering of proteins to RNAs using the bovine immunodeficiency virus-Tat peptide and BIV-TAR RNA.
abstract: To study the functions of RNA-binding proteins independent of their RNA-binding activity, tethering methods have been developed, based on the use of the RNA-binding domain of a well-characterized RNA-binding protein and its target RNA. Two bacteriophage proteins have mainly been used as tethers: the MS2 coat protein and the lambda N protein. Here we report an alternative system using the Tat (trans-activator) peptide from the bovine immunodeficiency virus (BIV), which binds to BIV-TAR (trans-activation response) RNA. We demonstrate the usefulness of this system by applying it to the analysis of the TNRC6B protein, a component of the microRNA-induced silencing complex.
authors.affiliation: RIKEN Systems and Structural Biology Center, Tsurumi, Yokohama 230-0045, Japan. waki@gsc.riken.jp
authors.forename: Motoaki
authors.initials: M
authors.lastname: Wakiyama
authors.forename: Yoko
authors.initials: Y
authors.lastname: Kaitsu
authors.forename: Reiko
authors.initials: R
authors.lastname: Muramatsu
authors.forename: Koji
authors.initials: K
authors.lastname: Takimoto
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002460:Cell Line; D015696:Gene Products, tat / Q000737:chemistry / Q000235:genetics*; D020868:Gene Silencing; D017930:Genes, Reporter; D006801:Humans; D016087:Immunodeficiency Virus, Bovine / Q000737:chemistry / Q000235:genetics*; D049410:Luciferases, Renilla; D008969:Molecular Sequence Data; D010957:Plasmids; D017434:Protein Structure, Tertiary; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics*; D016601:RNA-Binding Proteins / Q000032:analysis*; D014162:Transfection
chemical_list: D015696:Gene Products, tat; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D049410:Luciferases, Renilla