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Molecular characterization of the two‐component histidine kinase gene from Monilinia fructicola
Author(s) -
Ma Zhonghua,
Luo Yong,
Michailides Themis
Publication year - 2006
Publication title -
pest management science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.296
H-Index - 125
eISSN - 1526-4998
pISSN - 1526-498X
DOI - 10.1002/ps.1275
Subject(s) - mutant , histidine kinase , gene , virulence , biology , genetics , histidine , point mutation , protein kinase domain , amino acid
Abstract Brown rot of stone fruit caused by Monilinia fructicola (G. Wint) Honey is one of the most common fungal diseases in California. In this study, two laboratory‐induced iprodione‐resistant (LIR) mutants of M. fructicola were characterized by osmotic sensitivity, virulence on prune and sequence of the two‐component histidine kinase gene ( Mfos‐1 ). The LIR mutants showed more sensitivity to osmotic stress and lower virulence on prune than their wild‐type parent. Analysis of deduced amino acid of Mfos‐1 showed that this protein exhibited all the characteristic features of the two‐component histidine kinase genes, including osmotic sensing domain, six 90‐amino‐acid repeat motifs (coiled coil region) and kinase core and response regulator domains. Comparison of DNA sequences of the Mfos‐1 from LIR mutants and the wild‐type sensitive (S) isolate showed that LIR mutants had single point mutations in the coiled coil region of Mfos‐1 . Copyright © 2006 Society of Chemical Industry