RNA



REVIEW
REVIEW

Human ribonuclease P: Subunits, function, and intranuclear localization


NAYEF  JARROUS a1c1
a1 Department of Molecular Biology, The Hebrew University–Hadassah Medical School, Jerusalem 91120, Israel

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.

(Received July 19 2001)
(Revised August 22 2001)
(Accepted September 28 2001)


Key Words: Cajal bodies; catalytic ribonucleoprotein; nucleolus; RNase MRP; RNase P; tRNA.

Correspondence:
c1 Reprint requests to: Nayef Jarrous, Department of Molecular Biology, The Hebrew University–Hadassah Medical School, Jerusalem 91120, Israel; e-mail: jarrous@md.huji.ac.il.