| First Author | van Eenennaam H | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 34 | Pages | 31635-41 |
| PubMed ID | 11413139 | Mgi Jnum | J:71040 |
| Mgi Id | MGI:2149119 | Doi | 10.1074/jbc.M103399200 |
| Citation | van Eenennaam H, et al. (2001) hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases. J Biol Chem 276(34):31635-41 |
| abstractText | The RNase MRP and RNase P particles both function as endoribonucleases. RNase MRP has been implicated in the processing of precursor-rRNA, whereas RNase P has been shown to function in the processing of pre-tRNA. Both ribonucleoprotein particles have an RNA component that can be folded into a similar secondary structure and share several protein components. We have identified human, rat, mouse, cow, and Drosophila homologues of the Pop5p protein subunit of the yeast RNase MRP and RNase P complexes. The human Pop5 cDNA encodes a protein of 163 amino acids with a predicted molecular mass of 18.8 kDa. Polyclonal antibodies raised against recombinant hPop5 identified a 19-kDa polypeptide in HeLa cells and showed that hPop5 is associated with both RNase MRP and RNase P. Using affinity-purified anti-hPop5 antibodies, we demonstrated that the endogenous hPop5 protein is localized in the nucleus and accumulates in the nucleolus, which is consistent with its association with RNase MRP and RNase P. Catalytically active RNase P was partially purified from HeLa cells, and hPop5 was shown to be associated with it. Finally, the evolutionarily conserved acidic C-terminal tail of hPop5 appeared to be required neither for complex formation nor for RNase P activity. |
