Linked Life Data

1423663

Source:http://linkedlifedata.com/resource/pubmed/id/1423663

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-12-22
pubmed:abstractText
We report the cloning and sequencing of 18 mutant alleles of the benA, beta-tubulin gene of Aspergillus nidulans that confer resistance to the benzimidazole antifungal, antimicrotubule compounds benomyl, carbendazim, nocodazole, and thiabendazole. In 12 cases, amino acid 6 was changed from histidine to tyrosine or leucine. In four cases, amino acid 198 was changed from glutamic acid to aspartic acid, glutamine, or lysine. In two cases, amino acid 200 was altered from phenylalanine to tyrosine. These data, along with previous data indicating that amino acid 165 is involved in the binding of the R2 group of these compounds [Jung and Oakley, 1990: Cell Motil. Cytoskeleton 17:87-94], suggest that regions of beta-tubulin containing amino acids 6, 165, and 198-200 interact to form the binding site of benzimidazole antimicrotubule agents. These results also suggest that the presence of phenylalanine at amino acid 200 contributes to the great sensitivity of many fungi to benzimidazole antimicrotubule agents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0886-1544
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:geneSymbol
benA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
170-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Amino acid alterations in the benA (beta-tubulin) gene of Aspergillus nidulans that confer benomyl resistance.
pubmed:affiliation
Department of Molecular Genetics, Ohio State University, Columbus 43210.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.