Families of bacterial signal‐transducing proteins

Abstract

SummaryBacteria can respond to a variety of environmentai stimuli by means of systems generally composed of two proteins. The first protein (sensor or transmitter) is usually a transmembrane protein with cytoplasmic and extracytoplasmic domains. The extracytoplasmic domain (sensor) senses the environment and transfers the signal through the transmembrane domain to the cytoplasmic domain (transmitter), which has kinase activity. The second protein is located in the cytoplasm and contains an amino-terminal domain (receiver), which can be phosphorylated by the transmitter, and a carboxy-terminal region (regulator), which regulates gene expression by binding to DNA. The transmitter and receiver modules (the kinase and its target) are conserved in all signal-transducing systems and are the 'core structure' of this twocomponent system. The sensors and the regulators vary according to the stimuli they respond to and the DNA structure they interact with. On the basis of their sequence homology, the proteins belonging to such two-component systems can be classified into different families, which are summarized in this review.

Identification and sequence analysis of the hupR1 gene, which encodes a response regulator of the NtrC family required for hydrogenase expression in Rhodobacter capsulatus

“…Amino acid sequence comparisons indicated that the gene is capable of encoding a regulatory protein belonging to a superfamily of signal-transducing proteins. Use of a translational fusion between the lacZ gene and the promoter of the structural hydrogenase operon (hupSLp) confirmed that the product of the hupR1 gene is required for full activity of hupSLp.(A preliminary account of these results was presented orally at the Annual Meeting of the American Society for Microbiology in Anaheim, Calif., [13][14][15][16][17] May 1990. The sequence of the 5' terminus of the hupR1 gene has recently been published [31].)…”

“…(A preliminary account of these results was presented orally at the Annual Meeting of the American Society for Microbiology in Anaheim, Calif., [13][14][15][16][17] May 1990. The sequence of the 5' terminus of the hupR1 gene has recently been published [31].)…”

Soil bacterial community and functional shifts in response to altered snowpack in moist acidic tundra of northern Alaska

“…4). Enzyme activity is partially regulated by the rate of gene expression as well as by post-transcriptional regulating factors, which include environmental factors (Gross et al, 1989). MichaelisMenten enzyme kinetics are sensitive to temperature (German et al, 2012), increasing the maximum rate of enzyme activity (V max ) by increasing the catalytic constant of the reaction (Razavi et al, 2015).…”

The dnrO gene encodes a DNA-binding protein that regulates daunorubicin production in Streptomyces peucetius by controlling expression of the dnrN pseudo response regulator gene

“…The former gene encodes a positively acting transcription factor similar to the OmpR-PhoB superfamily of response regulators (Gross et al, 1989) and thus the SARP proteins (Wietzorrek & Bibb, 1997), whilst the jadR2 gene encodes a negatively acting repressor protein similar to known repressors like EnvR (Klein et al, 1991), TetC (Scholtmeier & Hillen, 1984) and TcmR (Guilfoile & Hutchinson, 1992). Disruption of jadR2 relieves the stress response needed to induce jadomycin production in the wild-type strain, and when a jadR2 mutant is cultured under stressful conditions (heat shock or toxic concentrations of ethanol), jadomycin is overproduced (Yang et al, 1995).…”

“…In contrast to typical bacterial response regulator proteins (Gross et al, 1989), DnrN does not appear to require phosphorylation for its activity even though it possesses a putative phosphorylation site (D55) and other highly conserved amino acid residues characteristic of response regulator proteins. In this regard, DnrN resembles the S. coelicolor RedZ protein that regulates redD transcription (Guthrie et al, 1998 ;White & Bibb, 1997).…”