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.

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Title Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo
Author(s) Dichtl, Bernhard
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
1460-2075
Keyword(s) POP3 gene
RNA processing
RNase MRP
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
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

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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