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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-8-5
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pubmed:abstractText |
NIN1 is an essential gene for growth of the yeast Saccharomyces cerevisiae and was recently found to encode a component of the regulatory subunit of the 26S proteasome. The nin1-1 mutant is temperature sensitive and its main defect is in G1/S progression and G2/M progression at non-permissive temperatures. One of the two multicopy suppressors of nin1-1, SUN2 (SUppressor of Nin1-1), was found to encode a protein of 523 amino acids whose sequence is similar to those of Drosophila melanogaster diphenol oxidase A2 and the mouse mast-cell Tum(-) transplantation antigen, P91A. The C-terminal half of Sun2p was found to be functional as Sun2p at 25 degrees C, 30 degrees C, and 34 degrees C but not at 37 degrees C. The open reading frame (ORF) of the Drosophila diphenol oxidase A2 gene (Dox-A2) was obtained from a lambda phage cDNA library using the polymerase chain reaction technique. The Dox-A2 ORF driven by the TDH3 promoter complemented the phenotype of a strain deleted for sun2. This Dox-A2-dependent strain was temperature sensitive and accumulated dumb-bell-shaped cells, with an undivided nucleus at the isthmus, after temperature upshift. This morphology is similar to that of nin1-1 cells kept at a restrictive temperature. These results suggest that SUN2 is a functional counterpart of Dox-A2 and that these genes play a pivotal role in the cell cycle in each organism.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catechol Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glyceraldehyde-3-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RPN12 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/transplantation antigen P91A, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0026-8925
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
146-52
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8668124-Amino Acid Sequence,
pubmed-meshheading:8668124-Animals,
pubmed-meshheading:8668124-Base Sequence,
pubmed-meshheading:8668124-Binding Sites,
pubmed-meshheading:8668124-Catechol Oxidase,
pubmed-meshheading:8668124-Cell Cycle Proteins,
pubmed-meshheading:8668124-DNA, Fungal,
pubmed-meshheading:8668124-Drosophila melanogaster,
pubmed-meshheading:8668124-Fungal Proteins,
pubmed-meshheading:8668124-Gene Expression Regulation, Fungal,
pubmed-meshheading:8668124-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:8668124-Histocompatibility Antigens,
pubmed-meshheading:8668124-Mice,
pubmed-meshheading:8668124-Molecular Sequence Data,
pubmed-meshheading:8668124-Open Reading Frames,
pubmed-meshheading:8668124-Phenotype,
pubmed-meshheading:8668124-Promoter Regions, Genetic,
pubmed-meshheading:8668124-Proteasome Endopeptidase Complex,
pubmed-meshheading:8668124-Repressor Proteins,
pubmed-meshheading:8668124-Saccharomyces cerevisiae,
pubmed-meshheading:8668124-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8668124-Sequence Homology, Amino Acid,
pubmed-meshheading:8668124-Suppression, Genetic,
pubmed-meshheading:8668124-Temperature
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pubmed:year |
1996
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pubmed:articleTitle |
A multicopy suppressor of nin1-1 of the yeast Saccharomyces cerevisiae is a counterpart of the Drosophila melanogaster diphenol oxidase A2 gene, Dox-A2.
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pubmed:affiliation |
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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