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

被引：48

作者：

Guerrier-Takada, C ^{[1
]}

Eder, PS ^{[1
]}

Gopalan, V ^{[1
]}

Altman, S ^{[1
]}

机构：

[1] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06511 USA

来源：

RNA | 2002年 / 8卷 / 03期

关键词：

molecular cloning; UV crosslinking;

D O I：

10.1017/S1355838202027954

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：290 / 295

页数：6

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