Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Query: EC:2.7.13.3 (
histidine kinase
)
2,405
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Halophilic archaea, such as eubacteria, use methyl-accepting chemotaxis proteins (MCPs) to sense their environment. We show here that BasT is a halobacterial transducer protein (Htp) responsible for chemotaxis towards five attractant amino acids. The C-terminus of the protein exhibits the highly conserved regions that are diagnostic for MCPs: the signalling domain for communication with the
histidine kinase
and the methylation sites that interact with the methylation/demethylation enzymes for adaptation. Hydropathy analysis predicts an enterobacterial-type transducer protein topology for BasT, with an extracellular putative ligand-binding domain flanked by two transmembrane helices and a cytoplasmic domain. BasT-inactivated mutant cells are missing a membrane protein radiolabelled with L-[methyl-3H]-methionine in wild-type cells, confirming that BasT is methylatable and membrane bound. Behavioural analysis of the basT mutant cells by capillary and chemical-in-plug assays demonstrates complete loss of chemotactic responses towards five (leucine, isoleucine, valine, methionine and cysteine) of the six attractant amino acids for Halobacterium salinarum, whereas they still respond to arginine. The volatile methyl group production assays also corroborate these findings and confirm that BasT signalling induces methyl group turnover. Our data identify BasT as the chemotaxis transducer protein for the branched chain amino acids leucine, isoleucine and valine as well as for methionine and cysteine. Thus, BasT and the arginine sensor
Car
cover the entire spectrum of chemotactic responses towards attractant amino acids in H. salinarum.
...
PMID:BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum. 1067 86
One hundred and eight isolates of Botrytis cinerea from greenhouse cucumber and tomato in two locations in Jiangsu Province (Nanjing and Huaiyin) and one location in Shandong Province were tested for their sensitivities to the four fungicides commonly used in China. Isolates with resistance to all four fungicides-carbendazim, diethofencarb, procymidone, and pyrimethanil (
Car
R
Die
R
Prc
R
Pyr
R
)-were found in all three regions in this study. High frequencies (52 and 53%) of resistance to all four fungicides were observed among the 62 isolates collected in Nanjing and the 36 isolates collected in Huaiyin in Jiangsu Province. The 10 isolates from Shandong Province were all resistant to the four fungicides. Pathogenicity and sporulation in vivo, and mycelial growth, sporulation, spore germination, and osmotic sensitivity to NaCl in vitro, were similar for the group of quadruple-resistant and wild-type isolates (P > 0.05). In the present study, the complete two-component
histidine kinase
gene (Bos1) was sequenced for 10 procymidone-resistant and 3 procymidone-sensitive B. cinerea isolates. Isolates representing four different procymidone-resistant phenotypes (
Car
R
Die
S
Prc
R
Pyr
S
,
Car
R
Die
R
Prc
R
Pyr
S
,
Car
R
Die
R
Prc
R
Pyr
R
, and
Car
R
Die
R
Prc
R
Pyr
R
) all had nucleic acid point mutations resulting in amino acid changes at position 369 (change from glutamine to proline) as well as at amino acid position 373 (asparagine to serine) in the Bos1 gene.
...
PMID:Multiple Resistance of Botrytis cinerea from Vegetable Crops to Carbendazim, Diethofencarb, Procymidone, and Pyrimethanil in China. 3075 66
