Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1992-12-4
pubmed:abstractText
Two multicopy suppressors of the cal1-1 mutation in the yeast Saccharomyces cerevisiae have been isolated and characterized. They are identical to the yeast RHO1 and RHO2 genes, which encode putative small GTP-binding proteins. Multiple copies of either RHO gene suppressed temperature-sensitive growth of the cal1-1 mutant but did not suppress the cal1 null mutant. Genetic analysis suggests that overproduction of either RHO gene product acts for activation of the CAL1 gene product.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alkyl and Aryl Transferases, http://linkedlifedata.com/resource/pubmed/chemical/CDC43 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/CHS3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chitin Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transferases, http://linkedlifedata.com/resource/pubmed/chemical/geranylgeranyltransferase type-I, http://linkedlifedata.com/resource/pubmed/chemical/rhoB GTP-Binding Protein
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0749-503X
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:geneSymbol
CAL1, CDC42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
735-41
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
RHO gene products, putative small GTP-binding proteins, are important for activation of the CAL1/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biology, Faculty of Science, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't