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Life Sciences Commons

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Genetics and Genomics

University of Nebraska - Lincoln

School of Biological Sciences: Faculty Publications

2005

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Full-Text Articles in Life Sciences

Upf1p, A Highly Conserved Protein Required For Nonsense-Mediated Mrna Decay, Interacts With The Nuclear Pore Proteins Nup100p And Nup116p, Tara Nazarenus, Rebecca Cedarberg, Ryan Bell, Joseph Cheatle, Amanda Forch, Alexis Haifley, Ann Hou, Bessie Wanja Kebaara, Christina Shields, Kate Stoysich, Rachel Taylor, Audrey L. Atkin Jan 2005

Upf1p, A Highly Conserved Protein Required For Nonsense-Mediated Mrna Decay, Interacts With The Nuclear Pore Proteins Nup100p And Nup116p, Tara Nazarenus, Rebecca Cedarberg, Ryan Bell, Joseph Cheatle, Amanda Forch, Alexis Haifley, Ann Hou, Bessie Wanja Kebaara, Christina Shields, Kate Stoysich, Rachel Taylor, Audrey L. Atkin

School of Biological Sciences: Faculty Publications

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 …