pubmed-article:10998244 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C0027923 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1564871 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1969657 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1624609 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
pubmed-article:10998244 | lifeskim:mentions | umls-concept:C0521060 | lld:lifeskim |
pubmed-article:10998244 | pubmed:issue | 36 | lld:pubmed |
pubmed-article:10998244 | pubmed:dateCreated | 2000-10-13 | lld:pubmed |
pubmed-article:10998244 | pubmed:abstractText | A new gene encoding a novel GATA factor, ASD4, of Neurospora crassa was isolated and demonstrated to possess one intron and to specify an open reading frame encoding a protein with 427 amino acid residues. The ASD4 protein contains a single GATA-type zinc finger and a putative coiled-coil domain. Unlike related proteins, DAL80 in yeast and NREB in Penicillium, ASD4 does not appear to be involved in regulation of nitrogen metabolism. An Asd-4 null mutant obtained by the rip procedure did not show any effect upon nitrogen control, but instead resulted in severe defects in ascus and ascospore genesis. The Asd-4 rip mutant is dominant to Asd-4+. A cross of the Asd-4 mutant with wild-type resulted in fruiting bodies that appeared to be normal macroscopically but which were complete devoid of asci and ascospores. Introduction of the Asd-4+ gene into the Asd-4 rip mutant corrected the defect in ascus and ascospore development in crosses with wild-type. Mobility shift assays demonstrated that ASD4 acts as a sequence-specific DNA binding protein and recognizes DNA fragments that contain GATA core elements. Gel filtration and cross-linking experiments revealed that the ASD4 protein exists as a tetramer in solution. These results suggest that the ASD4 protein functions positively as a transcriptional regulator of sexual development in Neurospora. | lld:pubmed |
pubmed-article:10998244 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998244 | pubmed:language | eng | lld:pubmed |
pubmed-article:10998244 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998244 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10998244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10998244 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10998244 | pubmed:month | Sep | lld:pubmed |
pubmed-article:10998244 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:10998244 | pubmed:author | pubmed-author:HaasHH | lld:pubmed |
pubmed-article:10998244 | pubmed:author | pubmed-author:MarzlufG AGA | lld:pubmed |
pubmed-article:10998244 | pubmed:author | pubmed-author:FengBB | lld:pubmed |
pubmed-article:10998244 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10998244 | pubmed:day | 12 | lld:pubmed |
pubmed-article:10998244 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:10998244 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10998244 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10998244 | pubmed:pagination | 11065-73 | lld:pubmed |
pubmed-article:10998244 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10998244 | pubmed:meshHeading | pubmed-meshheading:10998244... | lld:pubmed |
pubmed-article:10998244 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10998244 | pubmed:articleTitle | ASD4, a new GATA factor of Neurospora crassa, displays sequence-specific DNA binding and functions in ascus and ascospore development. | lld:pubmed |
pubmed-article:10998244 | pubmed:affiliation | Department of Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA. | lld:pubmed |
pubmed-article:10998244 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10998244 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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