title: The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation.
abstract: Most RNA polymerase III transcripts are bound immediately after synthesis by an abundant nuclear phosphoprotein known as the La autoantigen. Experiments performed in the budding yeast Saccharomyces cerevisiae have revealed that binding of the La protein to tRNA precursors is required for the endonucleolytic maturation of the 3' terminus of many tRNAs. In the absence of this protein, the 3' ends of these tRNAs are trimmed by exonucleases (Yoo CJ, Wolin SL, 1997, Cell 89:393-402). Here we report the characterization of the La protein in the fission yeast Schizosaccharomyces pombe. As was described for budding yeast, S. pombe cells lacking the La protein are viable and exhibit alterations in the pathway of pre-tRNA maturation. Introduction of either the human, S. cerevisiae, or S. pombe La protein into these cells restores the detected pattern of tRNA processing intermediates to that of wild-type cells. By performing immunoprecipitations from cells that were metabolically labeled with 32P-orthophosphate, we demonstrate that the S. pombe and S. cerevisiae La proteins, like the human La protein, are phosphorylated in vivo. Thus, although the La protein is dispensable for growth in these yeasts, both the structure of the protein and its function in pre-tRNA maturation have been highly conserved throughout evolution.
authors.affiliation: Department of Cell Biology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
authors.forename: D J
authors.initials: DJ
authors.lastname: Van Horn
authors.forename: C J
authors.initials: CJ
authors.lastname: Yoo
authors.forename: D
authors.initials: D
authors.lastname: Xue
authors.forename: H
authors.initials: H
authors.lastname: Shi
authors.forename: S L
authors.initials: SL
authors.lastname: Wolin
mesh_terms: D000595:Amino Acid Sequence; D001324:Autoantigens / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics / Q000502:physiology; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D010766:Phosphorylation; D012323:RNA Processing, Post-Transcriptional / Q000235:genetics*; D012331:RNA, Fungal / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D011993:Recombinant Fusion Proteins; D015183:Restriction Mapping; D012261:Ribonucleoproteins / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D012568:Schizosaccharomyces / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D000097585:SS-B Antigen
chemical_list: D001324:Autoantigens; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins; D010750:Phosphoproteins; D012331:RNA, Fungal; D012343:RNA, Transfer; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; D000097585:SS-B Antigen; C088396:LHP1 protein, S cerevisiae; C082265:SLA1 protein, S cerevisiae