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Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae.
- Source :
-
FEBS letters [FEBS Lett] 2012 Apr 24; Vol. 586 (8), pp. 1173-8. Date of Electronic Publication: 2012 Mar 24. - Publication Year :
- 2012
-
Abstract
- Addition of poly(A) to the 3' ends of cleaved pre-mRNA is essential for mRNA maturation and is catalyzed by Pap1 in yeast. We have previously shown that a non-viable Pap1 mutant lacking the first 18 amino acids is fully active for polyadenylation of oligoA, but defective for pre-mRNA polyadenylation, suggesting that interactions at the N-terminus are important for enzyme function in the processing complex. We have now identified proteins that interact specifically with this region. Cft1 and Pta1 are subunits of the cleavage/polyadenylation factor, in which Pap1 resides, and Nab6 and Sub1 are nucleic-acid binding proteins with known links to 3' end processing. Our results suggest a novel mechanism for controlling Pap1 activity, and possible models invoking these newly-discovered interactions are discussed.<br /> (Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Pancreatitis-Associated Proteins
Polynucleotide Adenylyltransferase genetics
Polynucleotide Adenylyltransferase metabolism
Protein Subunits chemistry
Protein Subunits genetics
Protein Subunits metabolism
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
mRNA Cleavage and Polyadenylation Factors genetics
mRNA Cleavage and Polyadenylation Factors metabolism
Poly A metabolism
Polynucleotide Adenylyltransferase chemistry
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins chemistry
mRNA Cleavage and Polyadenylation Factors chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 586
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 22575652
- Full Text :
- https://doi.org/10.1016/j.febslet.2012.03.036