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 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Ribonuclease P
Yeasts
RNA
RNA Precursors
Protein Subunits
Ligands

Keywords

  • POP3
  • RNase P
  • RPR1
  • RPR2

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology

Cite this

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

An active precursor in assembly of yeast nuclear ribonuclease P. / Srisawat, Chatchawan; Houser-Scott, Felicia; Bertrand, Edouard; Xiao, Shaohua; Singer, Robert H.; Engelke, David R.

In: RNA, Vol. 8, No. 10, 01.10.2002, p. 1348-1360.

Research output: Contribution to journalArticle

Srisawat, C, Houser-Scott, F, Bertrand, E, Xiao, S, Singer, RH & Engelke, DR 2002, 'An active precursor in assembly of yeast nuclear ribonuclease P', RNA, vol. 8, no. 10, pp. 1348-1360. https://doi.org/10.1017/S1355838202027048
Srisawat C, Houser-Scott F, Bertrand E, Xiao S, Singer RH, Engelke DR. An active precursor in assembly of yeast nuclear ribonuclease P. RNA. 2002 Oct 1;8(10):1348-1360. https://doi.org/10.1017/S1355838202027048
Srisawat, Chatchawan ; Houser-Scott, Felicia ; Bertrand, Edouard ; Xiao, Shaohua ; Singer, Robert H. ; Engelke, David R. / An active precursor in assembly of yeast nuclear ribonuclease P. In: RNA. 2002 ; Vol. 8, No. 10. pp. 1348-1360.
@article{bafb885c826148fbb320d583478c8a34,
title = "An active precursor in assembly of yeast nuclear ribonuclease P",
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.",
keywords = "POP3, RNase P, RPR1, RPR2",
author = "Chatchawan Srisawat and Felicia Houser-Scott and Edouard Bertrand and Shaohua Xiao and Singer, {Robert H.} and Engelke, {David R.}",
year = "2002",
month = "10",
day = "1",
doi = "10.1017/S1355838202027048",
language = "English (US)",
volume = "8",
pages = "1348--1360",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "10",

}

TY - JOUR

T1 - An active precursor in assembly of yeast nuclear ribonuclease P

AU - Srisawat, Chatchawan

AU - Houser-Scott, Felicia

AU - Bertrand, Edouard

AU - Xiao, Shaohua

AU - Singer, Robert H.

AU - Engelke, David R.

PY - 2002/10/1

Y1 - 2002/10/1

N2 - 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.

AB - 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.

KW - POP3

KW - RNase P

KW - RPR1

KW - RPR2

UR - http://www.scopus.com/inward/record.url?scp=0036792845&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036792845&partnerID=8YFLogxK

U2 - 10.1017/S1355838202027048

DO - 10.1017/S1355838202027048

M3 - Article

C2 - 12403471

AN - SCOPUS:0036792845

VL - 8

SP - 1348

EP - 1360

JO - RNA

JF - RNA

SN - 1355-8382

IS - 10

ER -