title: Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.
abstract: Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo. Here, we report that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme. Pop1/Pop6/Pop7 binding is specific and involves an RNA domain highly similar to a protein-binding domain in the RNAs of RNase P/MRP. The results also show that Pop1/Pop6/Pop7 function to maintain the essential components Est1 and Est2 on the RNA in vivo. Consistently, addition of Pop1 allows for telomerase activity reconstitution with wild-type telomerase RNA in vitro. Thus, the same chaperoning module has allowed the evolution of functionally and, remarkably, structurally distinct RNPs, telomerase, and RNases P/MRP from unrelated progenitor RNAs.
authors.affiliation: Department of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
authors.forename: Bruno
authors.initials: B
authors.lastname: Lemieux
authors.affiliation: Department of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
authors.forename: Nancy
authors.initials: N
authors.lastname: Laterreur
authors.affiliation: Department of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
authors.forename: Anna
authors.initials: A
authors.lastname: Perederina
authors.affiliation: Department of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
authors.forename: Jean-François
authors.initials: JF
authors.lastname: Noël
authors.affiliation: Department of Anatomy and Cellular Biology,Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada.
authors.forename: Marie-Line
authors.initials: ML
authors.lastname: Dubois
authors.affiliation: Department of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
authors.forename: Andrey S
authors.initials: AS
authors.lastname: Krasilnikov
authors.affiliation: Department of Microbiology and Infectious Diseases, Center of Excellence in RNA Biology, Université de Sherbrooke, Sherbrooke, QC J1E 4K8, Canada. Electronic address: raymund.wellinger@usherbrooke.ca.
authors.forename: Raymund J
authors.initials: RJ
authors.lastname: Wellinger
mesh_terms: D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D008958:Models, Molecular; D012331:RNA, Fungal / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D004718:Saccharomycetales / Q000201:enzymology*; D019098:Telomerase / Q000737:chemistry* / Q000378:metabolism
chemical_list: C089992:POP1 protein, S cerevisiae; D012331:RNA, Fungal; D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; C099024:EST1 protein, S cerevisiae; C509185:EST2 protein, S cerevisiae; D019098:Telomerase; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C000612025:POP6 protein, S cerevisiae; C000612026:POP7 protein, S cerevisiae; D043262:Ribonuclease P