Journal article
Saccharomyces cerevisiae Putative G Protein, Gtr1p, Which Forms Complexes With Itself and a Novel Protein Designated as Gtr2p, Negatively Regulates the Ran/Gsp1p G Protein Cycle Through Gtr2p
Genetics (Austin), v 152(3), pp 853-867
01 Jul 1999
PMID: 10388807
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Prp20p and Rna1p are GDP/GTP exchanging and GTPase-activating factors of Gsp1p, respectively, and their mutations, prp20-1 and rna1-1, can both be suppressed by Saccharomyces cerevisiae gtr1-11. We found that gtr1-11 caused a single amino acid substitution in Gtr1p, forming S20L, which is a putative GDP-bound mutant protein, while Gtr1p has been reported to bind to GTP alone. Consistently, gtr1-S20N, another putative GDP-bound mutant, suppressed both prp20-1 and rna1-1. On the other hand, gtr1-Q65L, a putative GTP-bound mutant, was inhibitory to prp20-1 and rna1-1. Thus, the role that Gtr1p plays in vivo appears to depend upon the nucleotide bound to it. Our data suggested that the GTP-bound Gtr1p, but not the GDP-bound Gtr1p, interacts with itself through its C-terminal tail. S. cerevisiae possesses a novel gene, GTR2, which is homologous to GTR1. Gtr2p interacts with itself in the presence of Gtr1p. The disruption of GTR2 suppressed prp20-1 and abolished the inhibitory effect of gtr1-Q65L on prp20-1. This finding, taken together with the fact that Gtr1p-S20L is a putative, inactive GDP-bound mutant, implies that Gtr1p negatively regulates the Ran/Gsp1p GTPase cycle through Gtr2p.
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Details
- Title
- Saccharomyces cerevisiae Putative G Protein, Gtr1p, Which Forms Complexes With Itself and a Novel Protein Designated as Gtr2p, Negatively Regulates the Ran/Gsp1p G Protein Cycle Through Gtr2p
- Creators
- Nobutaka Nakashima - Kyushu UniversityEishi Noguchi - Kyushu UniversityTakeharu Nishimoto - Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan
- Publication Details
- Genetics (Austin), v 152(3), pp 853-867
- Publisher
- Oxford University Press
- Number of pages
- 15
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000081341900004
- Scopus ID
- 2-s2.0-0032771639
- Other Identifier
- 991014878321004721
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- Genetics & Heredity