A MULTISUBUNIT 3'-END PROCESSING FACTOR FROM YEAST CONTAINING POLY(A)POLYMERASE AND HOMOLOGS OF THE SUBUNITS OF MAMMALIAN CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR

Citation
Pj. Preker et al., A MULTISUBUNIT 3'-END PROCESSING FACTOR FROM YEAST CONTAINING POLY(A)POLYMERASE AND HOMOLOGS OF THE SUBUNITS OF MAMMALIAN CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR, EMBO journal, 16(15), 1997, pp. 4727-4737
Citations number
41
Categorie Soggetti
Biology,"Cell Biology
Journal title
ISSN journal
02614189
Volume
16
Issue
15
Year of publication
1997
Pages
4727 - 4737
Database
ISI
SICI code
0261-4189(1997)16:15<4727:AM3PFF>2.0.ZU;2-6
Abstract
Polyadenylation is the second step in 3' end formation of most eukaryo tic mRNAs. In Saccharomyces cerevisiae, this step requires three trans -acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I), Here, we describe the purificatio n and subunit composition of a multiprotein complex containing Pap1p a nd PF I activities, PF I-Pap1p was purified to homogeneity by compleme ntation of extracts mutant in the Fip1p subunit of PF I, In addition t o Fip1p and Pap1p, the factor comprises homologues of all four subunit s of mammalian cleavage and polyadenylation specificity factor (CPSF), as web as Pta1p, which previously has been implicated in pre-tRNA pro cessing, and several as yet uncharacterized proteins, As expected for a PF I subunit, pta1-1 mutant extracts are deficient for polyadenylati on in vitro, PF I also appears to be functionally related to CPSF, as it polyadenylates a substrate RNA more efficiently than Pap1p alone, P ossibly, the observed interaction of the complex with RNA tethers Pap1 p to its substrate.