Upf1p, a Highly Conserved Protein Required for Nonsense-Mediated mRNA Decay, Interacts with the Nuclear Pore Proteins Nup100p and Nup116p

Authors

Tara Nazarenus, University of Nebraska-LincolnFollow
Rebecca Cedarberg, University of Nebraska-Lincoln
Ryan Bell, University of Nebraska-Lincoln
Joseph Cheatle, University of Nebraska-Lincoln
Amanda Forch, University of Nebraska-Lincoln
Alexis Haifley, University of Nebraska-Lincoln
Ann Hou, University of Nebraska-Lincoln
Bessie Wanja Kebaara, University of Nebraska-LincolnFollow
Christina Shields, University of Nebraska-Lincoln
Kate Stoysich, University of Nebraska-Lincoln
Rachel Taylor, University of Nebraska-Lincoln
Audrey L. Atkin, University of Nebraska-LincolnFollow

ORCID IDs

Bessie Kebaara

Document Type

Article

Date of this Version

2005

Citation

Gene 345 (2005), pp. 199–212.

doi:10.1016/j.gene.2004.10.005

Comments

Copyright © 2004 Elsevier B.V. Used by permission.

Abstract

Saccharomyces cerevisiae Upf1p is a 971-amino-acid protein that is required for the nonsense-mediated mRNA decay (NMD) pathway, a pathway that degrades mRNAs with premature translational termination codons. We have identified a two-hybrid interaction between Upf1p and the nuclear pore (Nup) proteins, Nup100p and Nup116p. Both nucleoporins predominantly localize to the cytoplasmic side of the nuclear pore and participate in mRNA transport. The two-hybrid interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is dependent on the presence of the C-terminal 158 amino acids of Upf1p. Nup100p and Nup116p can be coimmunoprecipitated from whole-cell extracts with Upf1p, confirming in vitro the interaction identified by the two-hybrid analysis. Finally, we see a genetic interaction between UPF1 and NUP100. The growth of upf1Δ, can1-100 cells is inhibited by canavanine. The deletion of NUP100 allows upf1Δ, can1-100 cells to grow in the presence of canavanine. Physiologically, the interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is significant because it suggests a mechanism to ensure that Upf1p associates with newly synthesized mRNA as it is transported from the nucleus to the cytoplasm prior to the pioneer round of translation.