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Permanent link (DOI): https://doi.org/10.7939/R32F7K02M

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Identification and analysis of Tef1p, a novel Rho1p-interacting protein Open Access

Descriptions

Other title
Subject/Keyword
Tef1p
membrane fusion
actin
Rho1p
Rho GTPase
vacuole fusion
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Bodman, James A. R.
Supervisor and department
Eitzen, Gary (Cell Biology)
LaPointe, Paul (Cell Biology)
Examining committee member and department
Rachubinski, Richard (Cell Biology)
Hughes, Sarah (Medical Genetics)
Department
Department of Cell Biology
Specialization

Date accepted
2014-01-23T11:16:30Z
Graduation date
2014-06
Degree
Master of Science
Degree level
Master's
Abstract
Rho GTPases act as molecular switches, occupying an active GTP or an inactive GDP-bound state. Rho1p, one member of the Rho family GTPases, has a role in the late stages of vacuole fusion through an unknown mechanism. We identified a ~50kDa Rho1p-interacting protein as Tef1p, a dual function GTPase with known roles in both protein translation and actin cytoskeletal organization. Tef1p is an aminoacyl-tRNA transferase in protein translation where GTP-bound Tef1p shuttles aminoacyl-charged tRNAs to ribosomes where they are transferred to the elongating peptide chain. Tef1p also binds actin filaments and organizes them into higher order cable structures such as stress fibers. We used nucleotide-state specific affinity pulldown methods to determine that Tef1p specifically interacts with Rho1p, but not as a downstream effector. The Tef1p::Rho1p interaction was calcium- dependent, suggesting that the interaction occurs late in membrane fusion. Our data suggest that Tef1p modulates Rho1p function, perhaps via complex formation.
Language
English
DOI
doi:10.7939/R32F7K02M
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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