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Rpp14 and Rpp29, two protein subunits of human ribonuclease P

Published online by Cambridge University Press:  01 February 1999

NAYEF JARROUS ,
PAUL S. EDER ,
DONNA WESOLOWSKI  and
SIDNEY ALTMAN
NAYEF JARROUS
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
PAUL S. EDER
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA Present address: Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
DONNA WESOLOWSKI
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
SIDNEY ALTMAN
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
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Abstract

In HeLa cells, the tRNA processing enzyme ribonuclease P (RNase P) consists of an RNA molecule associated with at least eight protein subunits, hPop1, Rpp14, Rpp20, Rpp25, Rpp29, Rpp30, Rpp38, and Rpp40. Five of these proteins (hPop1p, Rpp20, Rpp30, Rpp38, and Rpp40) have been partially characterized. Here we report on the cDNA cloning and immunobiochemical analysis of Rpp14 and Rpp29. Polyclonal rabbit antibodies raised against recombinant Rpp14 and Rpp29 recognize their corresponding antigens in HeLa cells and precipitate catalytically active RNase P. Rpp29 shows 23% identity with Pop4p, a subunit of yeast nuclear RNase P and the ribosomal RNA processing enzyme RNase MRP. Rpp14, by contrast, exhibits no significant homology to any known yeast gene. Thus, human RNase P differs in the details of its protein composition, and perhaps in the functions of some of these proteins, from the yeast enzyme.

Keywords

human RNase Pnuclear localization sequencesRNase MRPrRNAtRNA
Type
REPORT
Information
RNA , Volume 5 , Issue 2 , February 1999 , pp. 153 - 157
Copyright
1999 RNA Society

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