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Pest Manag Sci. 2010 Jun;66(6):627-33. doi: 10.1002/ps.1919.

A single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol in Xanthomonas oryzae pv. oryzae.

Author information

1
Shenzhen Entry-Exit Inspection and Quarantine Bureau, Futian, Shenzhen, PR China.

Abstract

BACKGROUND:

Xanthomonas oryzae pv. Oryzae Ishiyama, a causal agent of rice bacterial leaf blight, was found to be sensitive in vitro to the systemic fungicide amicarthiazol (2-amino-4-methylthiazole -5-carboxanilide), which is a potent inhibitor of succinate dehydrogenase (SDH, EC 1.3.99.1). This paper aimed to determine the molecular resistance mechanism of X. oryzae pv. oryzae to amicarthiazol.

RESULTS:

UV-induced resistant mutants of X. oryzae pv. oryzae to amicarthiazol were isolated. The activity of SDH in wild-type X. oryzae pv. oryzae was strongly inhibited by amicarthiazol, while that in resistant mutants was insensitive, although their SDH activity was decreased compared with the wild-type sensitive strain without amicarthiazol. A mutation of Histidine(229) (CAC) to Tyrosine(229) (TAC) was identified in sdhB, which encoded the iron-sulfur protein subunit of SDH. The sdhB from the mutant was ligated into a cosmid, pUFR034, to generate pUFR034RAX, which conferred resistance to amicarthiazol when transformed into the wild-type sensitive strain.

CONCLUSION:

A mutation of His(229) (CAC) to Tyr(229) (TAC) in SdhB was responsible for determining amicarthiazol resistance. .

PMID:
20201001
DOI:
10.1002/ps.1919
[Indexed for MEDLINE]

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