| First Author | Kim H | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 289 |
| Issue | 2 | Pages | 513-8 |
| PubMed ID | 11716503 | Mgi Jnum | J:255342 |
| Mgi Id | MGI:6114969 | Doi | 10.1006/bbrc.2001.5992, |
| Citation | Kim H, et al. (2001) Interaction of poly(A) polymerase with the 25-kDa subunit of cleavage factor I. Biochem Biophys Res Commun 289(2):513-8 |
| abstractText | Mammalian poly(A) polymerase (PAP), a key enzyme in the pre-mRNA 3''-end processing reaction, carries the catalytic domain in the N-terminal region, an RNA binding domain, two nuclear localization signals, and a serine/threonine-rich regulatory domain in the C-terminal region. Using LexA-based yeast two-hybrid screening, we identified a cDNA encoding the 25-kDa subunit of cleavage factor I (CFI-25) as a protein that interacts with the C-terminal region of mouse PAP. The glutathione S-transferase pull-down assay and the immunoprecipitation experiment revealed that PAP directly interacts with CFI-25 and that the C-terminal 69 residues of PAP and the N-terminal 60 residues of CFI-25 are sufficient for the interaction between CFI-25 and PAP. Since CFI is known to function in the assembly of the pre-mRNA 3''-processing complex, this interaction may play an important role in the assembly of the processing complex and/or in the regulation of PAP activity within the complex. |
