An active precursor in assembly of yeast nuclear ribonuclease P

Chatchawan Srisawat, Felicia Houser-Scott, Edouard Bertrand, Shaohua Xiao, Robert H. Singer, David R. Engelke

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

The RNA-protein subunit assembly of nuclear RNase P was investigated by specific isolation and characterization of the precursor and mature forms of RNase P using an RNA affinity ligand. Pre-RNase P was as active in pre-tRNA cleavage as mature RNase P, although it contained only seven of the nine proteins found in mature RNase P. Pop3p and Rpr2p were not required for maturation of the RPR1 RNA subunit and virtually absent from pre-RNase P, implying that they are dispensable for pre-tRNA substrate recognition and cleavage. The RNase P subunit assembly is likely to occur in the nucleolus, where both precursor and mature forms of RNase P RNA are primarily localized. The results provide insight into assembly of nuclear RNase P, and suggest pre-tRNA substrate recognition is largely determined by the RNA subunit.

Original languageEnglish (US)
Pages (from-to)1348-1360
Number of pages13
JournalRNA
Volume8
Issue number10
DOIs
StatePublished - Oct 1 2002

Keywords

  • POP3
  • RNase P
  • RPR1
  • RPR2

ASJC Scopus subject areas

  • Molecular Biology

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    Srisawat, C., Houser-Scott, F., Bertrand, E., Xiao, S., Singer, R. H., & Engelke, D. R. (2002). An active precursor in assembly of yeast nuclear ribonuclease P. RNA, 8(10), 1348-1360. https://doi.org/10.1017/S1355838202027048