Survey of mutations of a histidine kinase gene BcOS1 in dicarboximide-resistant field isolates of Botrytis cinerea

2006 ◽  
Vol 72 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Michiyo Oshima ◽  
Shinpei Banno ◽  
Kiyotsugu Okada ◽  
Taeko Takeuchi ◽  
Makoto Kimura ◽  
...  
Keyword(s):  
Botrytis Cinerea ◽  
Histidine Kinase ◽  
Kinase Gene ◽  
Field Isolates

scholarly journals A Point Mutation in the Two-Component Histidine Kinase BcOS-1 Gene Confers Dicarboximide Resistance in Field Isolates of Botrytis cinerea

2002 ◽  
Vol 92 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Michiyo Oshima ◽  
Makoto Fujimura ◽  
Shinpei Banno ◽  
Chigusa Hashimoto ◽  
Takayuki Motoyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Botrytis Cinerea ◽  
Amino Acid Substitution ◽  
Histidine Kinase ◽  
Tandem Repeats ◽  
Polymerase Chain Reaction Amplification ◽  
Amino Acid Sequences ◽  
Osmotic Sensitivity ◽  
Field Isolates

Partial DNA fragments of Botrytis cinerea field isolates encoding the putative osmosensor histidine kinase gene (BcOS1) were cloned by polymerase chain reaction amplification and the predicted amino acid sequences were compared between dicarboximide-sensitive and resistant field isolates. The predicted BcOS1p is highly homologous to osmosensor histidine kinase OS1p from Neurospora crassa including the N-terminal six tandem repeats of approximately 90 amino acids. Four dicarboximide-resistant isolates of B. cinerea (Bc-19, Bc-45, Bc-682, and Bc-RKR) contained a single base pair mutation in their BcOS1 gene that resulted in an amino acid substitution in the predicted protein. In these resistant isolates, codon 86 of the second repeat, which encodes an isoleucine residue in sensitive strains, was converted to a codon for serine. The mutation of Botrytis field resistant isolates was located on the second unit of tandem amino acid repeats of BcOS1p, whereas the point mutations of the fifth repeat of OS1p confer resistance to both dicarboximides and phenylpyrroles and also osmotic sensitivity in Neurospora crassa. These results suggest that an amino acid substitution within the second repeat of BcOS1p is responsible for phenotypes of field resistant isolates (resistant to dicarboximides but sensitive to phenylpyrroles, and normal osmotic sensitivity) in B. cinerea.

Detection of Botrytis cinerea field isolates with multiple fungicide resistance from table grape in Sicily

2015 ◽  
Vol 77 ◽  
pp. 65-73 ◽  
Author(s):  
Anna Panebianco ◽  
Ivana Castello ◽  
Gabriella Cirvilleri ◽  
Giancarlo Perrone ◽  
Filomena Epifani ◽  
...  
Keyword(s):  
Botrytis Cinerea ◽  
Fungicide Resistance ◽  
Table Grape ◽  
Field Isolates

scholarly journals Inactivation of the ciaH Gene in Streptococcus mutans Diminishes Mutacin Production and Competence Development, Alters Sucrose-Dependent Biofilm Formation, and Reduces Stress Tolerance

2004 ◽  
Vol 72 (8) ◽  
pp. 4895-4899 ◽  
Author(s):  
Fengxia Qi ◽  
Justin Merritt ◽  
Renate Lux ◽  
Wenyuan Shi
Keyword(s):  
Stress Tolerance ◽  
Streptococcus Mutans ◽  
Histidine Kinase ◽  
Dental Plaque ◽  
Biofilm Formation ◽  
Competence Development ◽  
Clinical Isolates ◽  
Peptide Antibiotics ◽  
Kinase Gene

ABSTRACT Many clinical isolates of Streptococcus mutans produce peptide antibiotics called mutacins. Mutacin production may play an important role in the ecology of S. mutans in dental plaque. In this study, inactivation of a histidine kinase gene, ciaH, abolished mutacin production. Surprisingly, the same mutation also diminished competence development, stress tolerance, and sucrose-dependent biofilm formation.

Molecular characterization of the two-component histidine kinase gene fromMonilinia fructicola

2006 ◽  
Vol 62 (10) ◽  
pp. 991-998 ◽  
Author(s):  
Zhonghua Ma ◽  
Yong Luo ◽  
Themis Michailides
Keyword(s):  
Molecular Characterization ◽  
Histidine Kinase ◽  
Kinase Gene ◽  
Two Component

alr0117, a two-component histidine kinase gene, is involved in heterocyst development in Anabaena sp. PCC 7120

Microbiology ◽  
2004 ◽  
Vol 150 (2) ◽  
pp. 447-453 ◽  
Author(s):  
Degang Ning ◽  
Xudong Xu
Keyword(s):  
Histidine Kinase ◽  
Regulatory System ◽  
Gene Encoding ◽  
Kinase Gene ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Anabaena Sp ◽  
Pcc 7120 ◽  
Polysaccharide Layer ◽  
Heterocyst Development

Anabaena sp. PCC 7120 was mutagenized by transposon Tn5-1087b, generating a mutant whose heterocysts lack the envelope polysaccharide layer. The transposon was located between nucleotides 342 and 343 of alr0117, a 918 bp gene encoding a histidine kinase for a two-component regulatory system. Complementation of the mutant with a DNA fragment containing alr0117 and targeted inactivation of the gene confirmed that alr0117 is involved in heterocyst development. RT-PCR showed that alr0117 was constitutively expressed in the presence or absence of a combined-nitrogen source. hepA and patB, the two genes turned on during wild-type heterocyst development, were no longer activated in an alr0117-null mutant. The two-component signal transduction system involving alr0117 may control the formation of the envelope polysaccharide layer and certain late events essential to the function of heterocysts.

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