Abstract
The polyadenylation factor subunit “Factor Interacting with Poly(A) polymerase” (Fip1) is an important bridging subunit in the eukaryotic polyadenylation complex. To better understand the functioning of Fip1 in Arabidopsis, a random combinatorial screen for peptides that interact with a conserved plant-specific domain in the protein was conducted. A search of the Arabidopsis proteome using these Fip1-binding peptides as queries resulted in the identification of a number of putative Fip1-interacting proteins. One of these was the polyadenylation factor subunit, CstF77. This purported interaction was confirmed by yeast two-hybrid and in vitro assays. Mutation of the motif identified in the phage display screen eliminated the interaction, corroborating the results of the phage display screen. The domain of CstF77 that interacts with Fip1 lies at its extreme C-terminus and is distinct from the part of CstF77 that binds CstF64. Taken together, these results suggest that Fip1 is situated near CstF64 in the polyadenylation complex.
Keywords: Fip1, CstF77, CstF64, polyadenylation, phage display
Protein & Peptide Letters
Title: The Interaction Between Two Arabidopsis Polyadenylation Factor Subunits Involves an Evolutionarily-Conserved Motif and Has Implications for the Assembly and Function of the Polyadenylation Complex
Volume: 15 Issue: 1
Author(s): Arthur G. Hunt and Balasubrahmanyam Addepalli
Affiliation:
Keywords: Fip1, CstF77, CstF64, polyadenylation, phage display
Abstract: The polyadenylation factor subunit “Factor Interacting with Poly(A) polymerase” (Fip1) is an important bridging subunit in the eukaryotic polyadenylation complex. To better understand the functioning of Fip1 in Arabidopsis, a random combinatorial screen for peptides that interact with a conserved plant-specific domain in the protein was conducted. A search of the Arabidopsis proteome using these Fip1-binding peptides as queries resulted in the identification of a number of putative Fip1-interacting proteins. One of these was the polyadenylation factor subunit, CstF77. This purported interaction was confirmed by yeast two-hybrid and in vitro assays. Mutation of the motif identified in the phage display screen eliminated the interaction, corroborating the results of the phage display screen. The domain of CstF77 that interacts with Fip1 lies at its extreme C-terminus and is distinct from the part of CstF77 that binds CstF64. Taken together, these results suggest that Fip1 is situated near CstF64 in the polyadenylation complex.
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Cite this article as:
Hunt G. Arthur and Addepalli Balasubrahmanyam, The Interaction Between Two Arabidopsis Polyadenylation Factor Subunits Involves an Evolutionarily-Conserved Motif and Has Implications for the Assembly and Function of the Polyadenylation Complex, Protein & Peptide Letters 2008; 15 (1) . https://dx.doi.org/10.2174/092986608783330431
DOI https://dx.doi.org/10.2174/092986608783330431 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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