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The ras-related YPT1 gene product in yeast: A GTP-binding protein that might be involved in microtubule organization
Affiliation:2. Zentrum für Molekulare Biologie Universität Heidelberg Im Neuenheimer Feld 282 D-6900 Heidelberg Federal Republic of Germany;3. Frontier Research Institute for Interdisciplinary Sciences, Sendai 980-8579, Japan;4. Graduate School of Biomedical Engineering, Sendai 980-8579, Japan;5. Department of Information and Intelligent Systems, Tohoku University, Sendai 980-8579, Japan;1. Department of Molecular and Medical Genetics, Oregon Health & Science University, Portland, OR;2. Computational Biology Program, Oregon Health & Science University, Portland, OR;3. Knight Cardiovascular Institute, Oregon Health & Science University, Portland, OR;4. Proteomics Shared Resource, Oregon Health & Science University, Portland, OR;5. Department of Biomedical Engineering, Oregon Health & Science University, Portland, OR;6. Cancer Early Detection & Advanced Research Center, Oregon Health & Science University, Portland, OR;7. Knight Cancer Institute, Oregon Health & Science University, Portland, OR;8. Department of Chemical Physiology & Biochemistry, Oregon Health & Science University, Portland, OR
Abstract:The 23.5 kd protein product of the ras-related YPT1 gene of S. cerevisiae was found to be essential for cell growth. The loss of YPT1 function, studied in cells with the YPT1 gene on chromosome VI regulated by the galactose-inducible GAL10 promoter, led to arrested cells that were multibudded and exhibited a complete disorganization of microtubules and an apparent loss of nuclear integrity. The YPT protein binds GTP specifically. GTP binding of the protein is essential for its intracellular function. The Asn121→lle substitution, generated by site-directed mutagenesis, had a dominant lethal phenotype, the expression of the mutant protein led to binucleated cells and abnormal spindles. In contrast to the S. cerevisiae RAS1 and RAS2 gene products, the YPT protein seems to be involved, directly or indirectly, in microtubule organization and function.
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