Hostname: page-component-cd9895bd7-jkksz Total loading time: 0 Render date: 2024-12-28T13:42:52.634Z Has data issue: false hasContentIssue false
  • English
  • Français

An active precursor in assembly of yeast nuclear ribonuclease P

Published online by Cambridge University Press:  03 October 2002

CHATCHAWAN SRISAWAT ,
FELICIA HOUSER-SCOTT ,
EDOUARD BERTRAND ,
SHAOHUA XIAO ,
ROBERT H. SINGER  and
DAVID R. ENGELKE
CHATCHAWAN SRISAWAT
Affiliation:
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA
FELICIA HOUSER-SCOTT
Affiliation:
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA
EDOUARD BERTRAND
Affiliation:
Institut de Genetique Moleculaire de Montpellier, IFR 24-Centre National de la Recherche Scientifique UMR 5535, 34000 Montpellier, France
SHAOHUA XIAO
Affiliation:
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA
ROBERT H. SINGER
Affiliation:
Department of Anatomy and Structural Biology and Cell Biology, Albert Einstein College of Medicine, New York, New York 10461, USA
DAVID R. ENGELKE
Affiliation:
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA
Get access

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

RNase PRPR2POP3RPR1
Type
Research Article
Information
RNA , Volume 8 , Issue 10 , October 2002 , pp. 1348 - 1360
Copyright
2002 RNA Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)