Abstract
RNase MRP is a ribonucleoprotein (RNP) particle which is involved in the processing of pre-rRNA at site A(3) 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. Over-expression of Pop3p fully suppresses the ts growth phenotype of the rrp2-1 allele at 34 degrees C and gives partial suppression at 37 degrees C, Depletion of Pop3p in vivo results in a phenotype characteristic of the loss of RNase MRP activity; A(3) 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 A(2), 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.
Original language | English |
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Pages (from-to) | 417-429 |
Number of pages | 13 |
Journal | EMBO Journal |
Volume | 16 |
Issue number | 2 |
DOIs | |
Publication status | Published - 15 Jan 1997 |