Rpp14 and Rpp29, two protein subunits of human ribonuclease P

Nayef Jarrous, Paul S. Eder, Donna Wesolowski, Sidney Altman

Research output: Contribution to journalArticle

45 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)153-157
Number of pages5
JournalRNA
Volume5
Issue number2
DOIs
StatePublished - Feb 1999
Externally publishedYes

Fingerprint

Ribonuclease P
Protein Subunits
HeLa Cells
Enzymes
Yeasts
Ribosomal RNA
Fungal Proteins
Ribonucleases
Transfer RNA
Organism Cloning
Proteins
Complementary DNA
RNA
Rabbits
Antigens
Antibodies
Genes

Keywords

  • Human RNase P
  • Nuclear localization sequences
  • RNase MRP
  • rRNA
  • tRNA

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology

Cite this

Rpp14 and Rpp29, two protein subunits of human ribonuclease P. / Jarrous, Nayef; Eder, Paul S.; Wesolowski, Donna; Altman, Sidney.

In: RNA, Vol. 5, No. 2, 02.1999, p. 153-157.

Research output: Contribution to journalArticle

Jarrous, Nayef ; Eder, Paul S. ; Wesolowski, Donna ; Altman, Sidney. / Rpp14 and Rpp29, two protein subunits of human ribonuclease P. In: RNA. 1999 ; Vol. 5, No. 2. pp. 153-157.
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