Differential binding of methyl benzimidazol-2-yl carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans.
作者： L. C. Davidse
DOI: 10.1083/JCB.72.1.174
关键词:
摘要: The antimitotic compound methyl benzimidazol-2-yl carbamate (MBC) formed a complex in vitro with protein present mycelial extracts of fungi. binding Aspergillus nidulans showed set properties which is unique for tubulin. Binding occurred rapidly at 4 degrees C and was competitively inhibited by oncodazole colchicine. Other inhibitors microtubule function such as podophyllotoxin, vinblastine sulfate, melatonin, griseofulvin did not interfere MBC. Electrophoretic analysis partially purified preparations the revealed presence proteins similar mobilities mammalian tubulin monomers. Hence it concluded that identical fungal effect MBC on growth mutant strains A. positively correlated affinity sites this compound. apparent constant from wild type estimated 4.5 X 10(5), resistant strain 3.7 10(4), increased sensitivity to 1.6 10(6) liters/mol. Mutants showing resistance are candidates have alterations structure. Affinity probably common mechanism Low 2.5 10(3)
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