TY - JOUR
T1 - Human ribonuclease P
T2 - Subunits, function, and intranuclear localization
AU - Jarrous, Nayef
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
KW - Cajal bodies
KW - Catalytic ribonucleoprotein
KW - Nucleolus
KW - RNase MRP
KW - RNase P
KW - tRNA
UR - http://www.scopus.com/inward/record.url?scp=0036210354&partnerID=8YFLogxK
U2 - 10.1017/S1355838202011184
DO - 10.1017/S1355838202011184
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C2 - 11871657
AN - SCOPUS:0036210354
SN - 1355-8382
VL - 8
SP - 1
EP - 7
JO - RNA
JF - RNA
IS - 1
ER -