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rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0022202,
umls-concept:C0038323,
umls-concept:C0042121,
umls-concept:C0185117,
umls-concept:C0204727,
umls-concept:C0205409,
umls-concept:C0295291,
umls-concept:C0439097,
umls-concept:C0446013,
umls-concept:C0450254,
umls-concept:C0679058,
umls-concept:C1071267,
umls-concept:C1138842,
umls-concept:C1425833,
umls-concept:C1547348,
umls-concept:C1547699,
umls-concept:C1687052,
umls-concept:C1705241,
umls-concept:C2700640,
umls-concept:C2911684
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pubmed:issue |
6
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|
pubmed:dateCreated |
1994-10-11
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pubmed:databankReference |
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pubmed:abstractText |
The Magnaporthe grisea ERG2 gene, encoding delta 8-->delta 7 sterol isomerase, was isolated from a genomic library by heterologous hybridization to a fragment of the Ustilago maydis ERG2 gene. The isolated gene contained a reading frame of 745 bp which encoded a protein of 221 amino acids. The coding region was interrupted by a single putative 79-bp-long intron. The deduced amino-acid sequence exhibited similarity to the ERG2 gene products of U. maydis and of Saccharomyces cerevisiae, particularly in the central region of the proteins. The NH2-terminal of all three proteins contained a long stretch of amino acids that were strongly hydrophobic, suggesting that they may function by anchoring the protein to a membrane surface. The M. grisea ERG2 gene complemented a U. maydis deletion mutant in which the ERG2 gene had been removed using a one-step gene replacement procedure. The delta 8-->delta 7 sterol isomerase produced by the M. grisea ERG2 gene exhibited a level of sensitivity to the sterol biosynthesis inhibitor, tridemorph, similar to that of the enzyme derived from the U. maydis ERG2 gene.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0172-8083
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
531-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8082205-Amino Acid Sequence,
pubmed-meshheading:8082205-Base Sequence,
pubmed-meshheading:8082205-Enzyme Induction,
pubmed-meshheading:8082205-Fungal Proteins,
pubmed-meshheading:8082205-Fungicides, Industrial,
pubmed-meshheading:8082205-Gene Expression Regulation, Fungal,
pubmed-meshheading:8082205-Genes, Fungal,
pubmed-meshheading:8082205-Mitosporic Fungi,
pubmed-meshheading:8082205-Molecular Sequence Data,
pubmed-meshheading:8082205-Morpholines,
pubmed-meshheading:8082205-Recombinant Fusion Proteins,
pubmed-meshheading:8082205-Sequence Alignment,
pubmed-meshheading:8082205-Sequence Homology, Amino Acid,
pubmed-meshheading:8082205-Steroid Isomerases,
pubmed-meshheading:8082205-Transformation, Genetic,
pubmed-meshheading:8082205-Ustilago
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pubmed:year |
1994
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pubmed:articleTitle |
Isolation of the ERG2 gene, encoding sterol delta 8-->delta 7 isomerase, from the rice blast fungus Magnaporthe grisea and its expression in the maize smut pathogen Ustilago maydis.
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pubmed:affiliation |
Department of Agricultural Sciences, University of Bristol, Long Ashton Research Station, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study
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