Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-26T16:01:30.807Z Has data issue: false hasContentIssue false
  • English
  • Français

Human ribonuclease P: Subunits, function, and intranuclear localization

Published online by Cambridge University Press:  11 January 2002

NAYEF JARROUS
NAYEF JARROUS
Affiliation:
Department of Molecular Biology, The Hebrew University–Hadassah Medical School, Jerusalem 91120, Israel
Get access

Abstract

Catalytic complexes of nuclear ribonuclease P (RNase P) ribonucleoproteins are composed of several protein subunits that appear to have specific roles in enzyme function in tRNA processing. This review describes recent progress made in the characterization of human RNase P, its relationship with the ribosomal RNA processing ribonucleoprotein RNase MRP, and the unexpected evolutionary conservation of its subunits. A new model for the biosynthesis of human RNase P is presented, in which this process is dynamic, transcription-dependent, and implicates functionally distinct nuclear compartments in tRNA biogenesis.

Keywords

Cajal bodiescatalytic ribonucleoproteinnucleolusRNase MRPRNase PtRNA
Type
REVIEW
Information
RNA , Volume 8 , Issue 1 , January 2002 , pp. 1 - 7
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.)