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A study on the molecular mechanism of resistance to amicarthiazol in Xanthomonas campestris pv. citri by Jun Li; Mingguo Zhou; Hongxia Li; Changjun Chen; Jianxing Wang; Yujun Zhang is a Agricultural and Biological Sciences article available to read on EtoBox.

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## Abstract Three amicarthiazol‐resistant mutants (Xuv10, Xuv20 and Xuv40) were obtained by UV induction and used in this study. Minimal inhibition concentrations (MICs) of amicarthiazol against the growth of mutants and wild‐type isolate were 400 and 100 μg ml^−1^ respectively. Inhibition by amicarthiazol of succinate dehydrogenase (SDH) activities of __Xanthomonas campestris__ pv. __citri__ (Hasse) Dye wild‐type isolate (Xcc) and three resistant mutants derived from this isolate were assayed using triphenyltetrazolium chloride (TTC). The SDH activities of these mutants were significantly lower than that of Xcc. The complete nucleotide sequences of four subunits (SdhA, SdhB, SdhC and SdhD) of succinate‐ubiquinone oxidoreductase (SQR) were cloned by polymerase chain reaction (PCR) amplification. An amino acid mutation (His~229~→ Leu~229~) in __sdh__B was found to confer resistance of __X. campestris__ pv. __citri__ to amicarthiazol. It is suggested that this mutation alters the SDH complex in some way that prevents binding of amicarthiazol. Copyright © 2006 Society of Chemical Industry

Who reads A study on the molecular mechanism of resistance to amicarthiazol in Xanthomonas campestris pv. citri?

Author

Jun Li; Mingguo Zhou; Hongxia Li; Changjun Chen; Jianxing Wang; Yujun Zhang

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1526-498X)

Published

2006

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)