Journal article
Site-directed mutagenesis of Saccharomyces cerevisiae β-tubulin: interaction between residue 167 and benzimidazole compounds
FEBS letters, v 385(1), pp 7-10
1996
PMID: 8641470
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Abstract
Benzimidazoles are widely used as anthelmintic agents and systemic fungicides. In susceptible organisms, benzimidazoles bind to β-tubulin and block microtubule polymerization. To further characterize this interaction, site-directed mutagenesis followed by gene replacement was used to change
Saccharomyces cerevisiae β-tubulin residue Phe-167 to Tyr. Consistent with previous studies, this mutation resulted in at least 3–4-fold decreased sensitivity to the benzimidazole derivatives carbendazim and nocodazole. The Tyr-167 mutant was cold sensitive, implying a direct effect on benzimidazole binding rather than a nonspecific increase in microtubule stability. Surprisingly, the mutant had 8-fold increased sensitivity to the derivative benomyl, which is structurally identical to carbendazim except at position 1. This suggests that residue 167 interacts with benzimidazoles in the vicinity of the 1-position.
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Details
- Title
- Site-directed mutagenesis of Saccharomyces cerevisiae β-tubulin: interaction between residue 167 and benzimidazole compounds
- Creators
- Jing LiSantosh K KatiyarThomas D Edlind
- Publication Details
- FEBS letters, v 385(1), pp 7-10
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:A1996UJ12500003
- Scopus ID
- 2-s2.0-0029889945
- Other Identifier
- 991014878040104721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics
- Cell Biology