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Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P

Published online by Cambridge University Press:  27 July 2001

NAYEF JARROUS
Affiliation:
Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel
ROBERT REINER
Affiliation:
Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel
DONNA WESOLOWSKI
Affiliation:
Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
HAGIT MANN
Affiliation:
Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel
CECILIA GUERRIER-TAKADA
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

Rpp21, a protein subunit of human nuclear ribonuclease P (RNase P) was cloned by virtue of its homology with Rpr2p, an essential subunit of Saccharomyces cerevisiae nuclear RNase P. Rpp21 is encoded by a gene that resides in the class I gene cluster of the major histocompatibility complex, is associated with highly purified RNase P, and binds precursor tRNA. Rpp21 is predominantly localized in the nucleoplasm but is also observed in nucleoli and Cajal bodies when expressed at high levels. Intron retention and splice-site selection in Rpp21 precursor mRNA regulate the intranuclear distribution of the protein products and their association with the RNase P holoenzyme. Our study reveals that dynamic nuclear structures that include nucleoli, the perinucleolar compartment and Cajal bodies are all involved in the production and assembly of human RNase P.

Type
Research Article
Copyright
© 2001 RNA Society

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