A bacterial basic region leucine zipper histidine kinase regulating toluene degradation

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TypeArticle
Journal titleProceedings of the National Academy of Sciences of the United States of America (PNAS)
Volume94
Issue4
Pages14531458; # of pages: 6
Subjectenv; two-component regulatory system; >signal transduction; aromatic hydrocarbons; Pseudomonas
AbstractThe two-component signal transduction pathways in bacteria use a histidine–aspartate phosphorelay circuit to mediate cellular changes in response to environmental stimuli. Here we describe a novel two-component todST system, which activates expression of the toluene degradation (tod) pathway in Pseudomonas putida F1. The todS gene is predicted to encode a sensory hybrid kinase with two unique properties—a basic region leucine zipper dimerization motif at the N terminus and a duplicated histidine kinase motif. Evidence from a synthetic peptide model suggests that TodS binds as a dimer to a pseudopalindromic sequence (5'-TGACTCA), which resembles the recognition sequence of the eukaryotic transcription factors Fos and Jun. These results provide additional evidence that bacteria and eukaryotes share common regulatory motifs. The todT gene product, a response regulator, was overproduced as a fusion protein in Escherichia coli, and the purified protein was found to bind specifically to a 6-bp palindromic DNA structure in the tod control region. The phosphorylated form of TodT appears to be the activator of tod structural genes. This is the first report of a two-component system that regulates aromatic metabolism in bacteria.
Publication date
Linkhttp://www.pnas.org/content/94/4/1453.short
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NoteUI - 97188489
Peer reviewedNo
NRC number40468
NPARC number3538647
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Record identifier2bcb70a5-fb97-47a1-864e-ea6c502fbe7a
Record created2009-03-01
Record modified2016-05-09
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