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

  • RNA. 2002 Mar;8(3):290-5. doi: 10.1017/s1355838202027954.
Cecilia Guerrier-Takada  1 ,  Paul S Eder ,  Venkat Gopalan ,  Sidney Altman
Affiliations
  • 1. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA.
PMID: 12003489 DOI: 10.1017/s1355838202027954
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.