Source:http://linkedlifedata.com/resource/pubmed/id/10931277
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
2000-12-1
|
| pubmed:databankReference | |
| pubmed:abstractText |
DopA is the founding member of a novel protein family required for correct cell morphology and spatiotemporal organization of multicellular structures in the filamentous fungus Aspergillus nidulans. DopA homologues from Saccharomyces cerevisiae (Dop1), Candida albicans, Caenorhabditis elegans, Rattus norvegicus and Homo sapiens have been identified from genome sequencing projects. S. cerevisiae DOP1 is essential for viability and, like DopA, affects cellular morphogenesis. dopA encodes a large protein (207 kDa) containing several putative domains, including three leucine zipper-like domains. Strains with either the temperature-sensitive dopA1(ts) allele, which alters one of the leucine zippers, or the null deltadopA allele, had abnormal morphology of the vegetative hyphae, delayed and asynchronous initiation of asexual development, aberrant morphogenesis of the conidiophore and an early block in the sexual cycle. The expression patterns of key transcriptional regulators of the asexual and sexual cycle (brlA, abaA and steA) are altered in a deltadopA background, suggesting that DopA functions upstream in the developmental pathway. Double mutant analysis showed that dopA interacts genetically with constitutively active and inactive forms of A. nidulans Aras to modulate hyphal morphogenesis and asexual development.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0950-382X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
36
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1250-64
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10931277-Amino Acid Sequence,
pubmed-meshheading:10931277-Animals,
pubmed-meshheading:10931277-Aspergillus nidulans,
pubmed-meshheading:10931277-Caenorhabditis elegans,
pubmed-meshheading:10931277-Candida albicans,
pubmed-meshheading:10931277-Cloning, Molecular,
pubmed-meshheading:10931277-Fungal Proteins,
pubmed-meshheading:10931277-Gene Deletion,
pubmed-meshheading:10931277-Genes, Fungal,
pubmed-meshheading:10931277-Hominidae,
pubmed-meshheading:10931277-Humans,
pubmed-meshheading:10931277-Leucine Zippers,
pubmed-meshheading:10931277-Molecular Sequence Data,
pubmed-meshheading:10931277-Morphogenesis,
pubmed-meshheading:10931277-Rats,
pubmed-meshheading:10931277-Saccharomyces cerevisiae,
pubmed-meshheading:10931277-Sequence Homology, Amino Acid,
pubmed-meshheading:10931277-Transcription, Genetic,
pubmed-meshheading:10931277-Yeasts
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Morphogenesis in Aspergillus nidulans requires Dopey (DopA), a member of a novel family of leucine zipper-like proteins conserved from yeast to humans.
|
| pubmed:affiliation |
Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow 83844, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|