TY - JOUR
T1 - A protein subunit of human RNase P, Rpp14, and its interacting partner, OIP2, have 3′→5′ exoribonuclease activity
AU - Jiang, Taijiao
AU - Altman, Sidney
PY - 2002/4/16
Y1 - 2002/4/16
N2 - The processing of precursor tRNAs at their 5′ and 3′ termini is a fundamental event in the biosynthesis of tRNA. RNase P is generally responsible for endonucleolytic removal of a leader sequence of precursor tRNA to generate the mature 5′ terminus. However, much less is known about the RNase P counterparts or other proteins that are active at the tRNA 3′ terminus. Here we show that one of the human RNase P subunits, Rpp14, together with one of its interacting protein partners, OIP2, is a 3′→5′ exoribonuclease with a phosphorolytic activity that processes the 3′ terminus of precursor tRNA. Immunoprecipitates of a crude human RNase P complex can process both ends of precursor tRNA by hydrolysis, but purified RNase P has no exonuclease activity. Rpp14 and OIP2 may be part of an exosome activity.
AB - The processing of precursor tRNAs at their 5′ and 3′ termini is a fundamental event in the biosynthesis of tRNA. RNase P is generally responsible for endonucleolytic removal of a leader sequence of precursor tRNA to generate the mature 5′ terminus. However, much less is known about the RNase P counterparts or other proteins that are active at the tRNA 3′ terminus. Here we show that one of the human RNase P subunits, Rpp14, together with one of its interacting protein partners, OIP2, is a 3′→5′ exoribonuclease with a phosphorolytic activity that processes the 3′ terminus of precursor tRNA. Immunoprecipitates of a crude human RNase P complex can process both ends of precursor tRNA by hydrolysis, but purified RNase P has no exonuclease activity. Rpp14 and OIP2 may be part of an exosome activity.
KW - Exosome
KW - Phosphorolytic enzymes
KW - tRNA processing
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U2 - 10.1073/pnas.072083699
DO - 10.1073/pnas.072083699
M3 - Article
C2 - 11929972
AN - SCOPUS:0037117474
SN - 0027-8424
VL - 99
SP - 5295
EP - 5300
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 8
ER -