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

Published online by Cambridge University Press:  24 April 2002

CECILIA GUERRIER-TAKADA ,
PAUL S. EDER ,
VENKAT GOPALAN  and
SIDNEY ALTMAN
CECILIA GUERRIER-TAKADA
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
PAUL S. EDER
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
VENKAT GOPALAN
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
SIDNEY ALTMAN
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA
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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.

Keywords

molecular cloningUV crosslinking
Type
REPORT
Information
RNA , Volume 8 , Issue 3 , March 2002 , pp. 290 - 295
Copyright
© 2002 RNA Society

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