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Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P

Published online by Cambridge University Press:  01 April 1998

NAYEF JARROUS ,
PAUL S. EDER ,
CECILIA GUERRIER-TAKADA ,
CHRISTER HOOG  and
SIDNEY ALTMAN
NAYEF JARROUS
Affiliation:
Department of Biology, Yale University, New Haven, Connecticut 06520, USA
PAUL S. EDER
Affiliation:
Department of 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.
CECILIA GUERRIER-TAKADA
Affiliation:
Department of Biology, Yale University, New Haven, Connecticut 06520, USA
CHRISTER HOOG
Affiliation:
Department of Cell and Molecular Biology, Karolinska Institute, S-17177 Stockholm, Sweden
SIDNEY ALTMAN
Affiliation:
Department of Biology, Yale University, New Haven, Connecticut 06520, USA
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Abstract

At least six proteins co-purify with human ribonuclease P (RNase P), a tRNA processing ribonucleoprotein. Two of these proteins, Rpp30 and Rpp38, are Th autoantigens. Recombinant Rpp30 and Rpp38 are also recognized by Th sera from systemic sclerosis patients. Two of the other proteins associated with RNase P, Rpp20 and Rpp40, do not cross-react with Th sera. Polyclonal antibodies raised against all four recombinant proteins recognize the corresponding proteins associated with RNase P and precipitate active holoenzyme. Catalytically active RNase P holoenzyme can be separated from the nucleolar and mitochondrial RNA processing endoribonuclease, RNase MRP, even though these two enzymes may share some subunits.

Keywords

auto-antigenshuman RNase Pnuclear localization sequencesRNase MRP
Type
Research Article
Information
RNA , Volume 4 , Issue 4 , April 1998 , pp. 407 - 417
Copyright
© 1998 RNA Society

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