TY - JOUR
T1 - Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P
AU - Guerrier-Takada, Cecilia
AU - Eder, Paul S.
AU - Gopalan, Venkat
AU - Altman, Sidney
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
KW - Molecular cloning
KW - UV crosslinking
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UR - http://www.scopus.com/inward/citedby.url?scp=0036223840&partnerID=8YFLogxK
U2 - 10.1017/S1355838202027954
DO - 10.1017/S1355838202027954
M3 - Article
C2 - 12003489
AN - SCOPUS:0036223840
SN - 1355-8382
VL - 8
SP - 290
EP - 295
JO - RNA
JF - RNA
IS - 3
ER -