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Interaction between Ran and Mog1 is required for efficient nuclear protein import.
R P Baker1, M T Harreman, J F Eccleston
1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom.
The Journal of Biological Chemistry
|August 18, 2001
Summary
Mog1 protein binding to Ran GTPase is essential for nuclear import in yeast. Disrupting this interaction causes defects in protein transport and cell growth, highlighting Mog1
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Mog1 is a nuclear protein interacting with Ran GTPase, crucial for nuclear transport directionality.
- Saccharomyces cerevisiae lacking MOG1 (Deltamog1) exhibits temperature-sensitive growth and nuclear import defects.
Purpose of the Study:
- To investigate the functional role of the Mog1-Ran interaction in nuclear protein import.
- To identify specific residues mediating the Mog1-Ran interaction and their impact on function.
Main Methods:
- Biochemical assays to study Mog1's effect on Ran nucleotide binding and release.
- Engineering of yeast strains with specific Mog1 and Ran mutants to disrupt their interaction.
- Phenotypic analysis of mutant strains, including growth assays and reporter protein localization.
Main Results:
- Mog1 binds to nucleotide-free Ran, promoting nucleotide release and forming a stable complex.
- Specific mutations in conserved residues (Mog1p Asp62, Glu65; yeast Ran Lys136) disrupt the Mog1-Ran interaction.
- Mutations impairing Mog1-Ran binding lead to temperature sensitivity and nuclear import defects, mirroring Deltamog1 phenotypes.
Conclusions:
- The Mog1-Ran interaction is critical for Mog1's function in nuclear protein import.
- Efficient nuclear protein import in vivo necessitates the physical interaction between Mog1 and Ran.