Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo

Dichtl, Bernhard and Tollervey, David 1997, Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo, EMBO journal, vol. 16, no. 2, pp. 417-429, doi: 10.1093/emboj/16.2.417.

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Title Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo
Author(s) Dichtl, BernhardORCID iD for Dichtl, Bernhard orcid.org/0000-0001-5514-4982
Tollervey, David
Journal name EMBO journal
Volume number 16
Issue number 2
Start page 417
End page 429
Total pages 13
Publisher Nature Publishing Group
Place of publication London, England
Publication date 1997-01-15
ISSN 0261-4189
Keyword(s) POP3 gene
RNA processing
RNase P
Saccharomyces cerevisiae
Summary RNase MRP is a ribonucleoprotein (RNP) particle which is involved in the processing of pre-rRNA at site A3 in internal transcribed spacer 1. Although RNase MRP has been analysed functionally, the structure and composition of the particle are not well characterized. A genetic screen for mutants which are synthetically lethal (sl) with a temperature-sensitive (ts) mutation in the RNA component of RNase MRP (rrp2-1) identified an essential gene, POP3, which encodes a basic protein of 22.6 kDa predicted molecular weight. Overexpression of Pop3p fully suppresses the ts growth phenotype of the rrp2-1 allele at 34°C and gives partial suppression at 37°C. Depletion of Pop3p in vivo results in a phenotype characteristic of the loss of RNase MRP activity; A3 cleavage is inhibited, leading to under-accumulation of the short form of the 5.8S rRNA (5.8SS) and formation of an aberrant 5.8S rRNA precursor which is 5'-extended to site A2. Pop3p depletion also inhibits pre-tRNA processing; tRNA primary transcripts accumulate, as well as spliced but 5'- and 3'-unprocessed pre-tRNAs. The Pop3p depletion phenotype resembles those previously described for mutations in components of RNase MRP and RNase P (rrp2-1, rpr1-1 and pop1-1). Immunoprecipitation of epitope-tagged Pop3p co-precipitates the RNA components of both RNase MRP and RNase P. Pop3p is, therefore, a common component of both RNPs and is required for their enzymatic functions in vivo. The ubiquitous RNase P RNP, which has a single protein component in Bacteria and Archaea, requires at least two protein subunits for its function in eukaryotic cells.
Language eng
DOI 10.1093/emboj/16.2.417
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©1997, Nature Publishing Group
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039327

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