title: A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts.
abstract: The first protein that binds to all newly synthesized RNA polymerase III transcripts is a highly conserved phosphoprotein known as the La autoantigen. Although binding by the yeast La protein Lhp1p to pre-tRNAs is required for the normal pathway of tRNA maturation, the role of the La protein in the biogenesis of other polymerase III transcripts has been unclear. We identified a mutation in a novel component of the U6 snRNP that causes yeast cells to require Lhp1p for growth. This protein, Lsm8p, is a member of a family of proteins, known as Sm-like proteins, that shares two conserved motifs with the core Sm proteins of the U1, U2, U4 and U5 snRNPs. The lsm8-1 cells have drastically reduced levels of the mature U6 snRNP, consistent with a defect in U6 snRNP assembly. In these cells, Lhp1p stabilizes newly synthesized U6 RNA, thus facilitating assembly of the RNA into the U6 snRNP. These results provide evidence that Lhp1p is a molecular chaperone for polymerase III-transcribed RNAs and implicate Lsm8p as a key component in the very early steps of U6 snRNP assembly.
authors.affiliation: Departments of Cell Biology, Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.
authors.forename: B K
authors.initials: BK
authors.lastname: Pannone
authors.forename: D
authors.initials: D
authors.lastname: Xue
authors.forename: S L
authors.initials: SL
authors.lastname: Wolin
mesh_terms: D000595:Amino Acid Sequence; D001324:Autoantigens / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D018628:Gene Dosage; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D063211:N-Terminal Acetyltransferase C; D012320:RNA Polymerase III / Q000096:biosynthesis* / Q000235:genetics; D012322:RNA Precursors / Q000378:metabolism; D012331:RNA, Fungal / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D017414:Ribonucleoprotein, U4-U6 Small Nuclear / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*; D017411:Ribonucleoproteins, Small Nuclear; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D055517:snRNP Core Proteins; D000097585:SS-B Antigen
chemical_list: D001324:Autoantigens; D005656:Fungal Proteins; D018832:Molecular Chaperones; D063211:N-Terminal Acetyltransferase C; D012320:RNA Polymerase III; D012322:RNA Precursors; D012331:RNA, Fungal; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D017414:Ribonucleoprotein, U4-U6 Small Nuclear; D012261:Ribonucleoproteins; D017411:Ribonucleoproteins, Small Nuclear; D029701:Saccharomyces cerevisiae Proteins; D055517:snRNP Core Proteins; D000097585:SS-B Antigen; C088396:LHP1 protein, S cerevisiae; C117009:NAA38 protein, human