Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.

V. Stolc, Sidney Altman

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The gene for an essential protein subunit of nuclear RNase P from Saccharomyces cerevisiae has been cloned. The gene for this protein, RPP1, was identified by virtue of its homology with a human scleroderma autoimmune antigen, Rpp30, which copurifies with human RNase P. Epitope-tagged Rpp1 can be found in association with both RNase P RNA and a related endoribonuclease, RNase MRP RNA, in immunoprecipitates from crude extracts of cells. Depletion of Rpp1 in vivo leads to the accumulation of precursor tRNAs with unprocessed 5' and 3' termini and reveals rRNA processing defects that have not been described previously for proteins associated with RNase P or RNase MRP. Immunoprecipitated complexes cleave both yeast precursor tRNAs and precursor rRNAs.

Original languageEnglish (US)
Pages (from-to)2926-2937
Number of pages12
JournalGenes and Development
Volume11
Issue number21
StatePublished - Nov 1 1997
Externally publishedYes

Fingerprint

Ribonuclease P
RNA Precursors
Protein Subunits
Saccharomyces cerevisiae
Ribonucleases
Endoribonucleases
RNA
Proteins
Complex Mixtures
Epitopes
Yeasts
Antigens

ASJC Scopus subject areas

  • Developmental Biology
  • Genetics

Cite this

@article{b1121751c54c4c5a8cc76b3825faa4ab,
title = "Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.",
abstract = "The gene for an essential protein subunit of nuclear RNase P from Saccharomyces cerevisiae has been cloned. The gene for this protein, RPP1, was identified by virtue of its homology with a human scleroderma autoimmune antigen, Rpp30, which copurifies with human RNase P. Epitope-tagged Rpp1 can be found in association with both RNase P RNA and a related endoribonuclease, RNase MRP RNA, in immunoprecipitates from crude extracts of cells. Depletion of Rpp1 in vivo leads to the accumulation of precursor tRNAs with unprocessed 5' and 3' termini and reveals rRNA processing defects that have not been described previously for proteins associated with RNase P or RNase MRP. Immunoprecipitated complexes cleave both yeast precursor tRNAs and precursor rRNAs.",
author = "V. Stolc and Sidney Altman",
year = "1997",
month = "11",
day = "1",
language = "English (US)",
volume = "11",
pages = "2926--2937",
journal = "Genes and Development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "21",

}

TY - JOUR

T1 - Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.

AU - Stolc, V.

AU - Altman, Sidney

PY - 1997/11/1

Y1 - 1997/11/1

N2 - The gene for an essential protein subunit of nuclear RNase P from Saccharomyces cerevisiae has been cloned. The gene for this protein, RPP1, was identified by virtue of its homology with a human scleroderma autoimmune antigen, Rpp30, which copurifies with human RNase P. Epitope-tagged Rpp1 can be found in association with both RNase P RNA and a related endoribonuclease, RNase MRP RNA, in immunoprecipitates from crude extracts of cells. Depletion of Rpp1 in vivo leads to the accumulation of precursor tRNAs with unprocessed 5' and 3' termini and reveals rRNA processing defects that have not been described previously for proteins associated with RNase P or RNase MRP. Immunoprecipitated complexes cleave both yeast precursor tRNAs and precursor rRNAs.

AB - The gene for an essential protein subunit of nuclear RNase P from Saccharomyces cerevisiae has been cloned. The gene for this protein, RPP1, was identified by virtue of its homology with a human scleroderma autoimmune antigen, Rpp30, which copurifies with human RNase P. Epitope-tagged Rpp1 can be found in association with both RNase P RNA and a related endoribonuclease, RNase MRP RNA, in immunoprecipitates from crude extracts of cells. Depletion of Rpp1 in vivo leads to the accumulation of precursor tRNAs with unprocessed 5' and 3' termini and reveals rRNA processing defects that have not been described previously for proteins associated with RNase P or RNase MRP. Immunoprecipitated complexes cleave both yeast precursor tRNAs and precursor rRNAs.

UR - http://www.scopus.com/inward/record.url?scp=0031278314&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031278314&partnerID=8YFLogxK

M3 - Article

C2 - 9353260

AN - SCOPUS:0031278314

VL - 11

SP - 2926

EP - 2937

JO - Genes and Development

JF - Genes and Development

SN - 0890-9369

IS - 21

ER -