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

Nayef Jarrous, Paul S. Eder, Cecilia Guerrier-Takada, Christer Hoog, Sidney Altman

Research output: Contribution to journalArticle

43 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)407-417
Number of pages11
JournalRNA
Volume4
Issue number4
StatePublished - Apr 1 1998
Externally publishedYes

Keywords

  • Auto-antigens
  • Human RNase P
  • Nuclear localization sequences
  • RNase MRP

ASJC Scopus subject areas

  • Molecular Biology

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  • Cite this

    Jarrous, N., Eder, P. S., Guerrier-Takada, C., Hoog, C., & Altman, S. (1998). Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P. RNA, 4(4), 407-417.