Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P

Cecilia Guerrier-Takada, Paul S. Eder, Venkat Gopalan, Sidney Altman

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

In HeLa cells, ribonuclease P (RNase P), the tRNA processing enzyme consists of an RNA subunit (H1 RNA) associated with at least nine protein subunits, Rpp14, Rpp20, Rpp21, Rpp29 (hPop4), Rpp30, Rpp38, Rpp40, hPop1, and hPop5 (18.8 kDa). We report here the cloning and immuno-biochemical analysis of Rpp25, another protein subunit of RNase P. Polyclonal rabbit antibodies raised against recombinant Rpp25 recognize their corresponding antigens in RNase P-containing fractions purified from HeLa cells, and they also precipitate active holoenzyme. Furthermore, this protein has general RNA binding properties.

Original languageEnglish (US)
Pages (from-to)290-295
Number of pages6
JournalRNA
Volume8
Issue number3
DOIs
StatePublished - Apr 25 2002
Externally publishedYes

Keywords

  • Molecular cloning
  • UV crosslinking

ASJC Scopus subject areas

  • Molecular Biology

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