Article
Fip1 regulates the activity of Poly(A) polymerase through multiple interactions.
Molecular and cellular biology - 1 Mar 2001
Helmling S, Zhelkovsky A, Moore C L
Abstract excerpt
Fip1 is an essential component of the Saccharomyces cerevisiae polyadenylation machinery and the only protein known to interact directly with poly(A) polymerase (Pap1). Its association with Pap1 inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain (C-RBD) of Pap1. We present here the identification of separate functional domains of Fip1. Amino...
Topics
- Amino Acid Transport Systems
- Cell Division
- Cell Survival
- Genetic Complementation Test
- Membrane Proteins
- Mutation
- Pancreatitis-Associated Proteins
- Polynucleotide Adenylyltransferase
- Protein Structure, Tertiary
- RNA-Binding Proteins