Construction of <i>lac</i> fusions to the inducible arginine‐and lysine decarboxylase genes of <i>Escherichia coli</i> K12

Auger, Elizabeth A.; Redding, Kevin; Plumb, Troy J.; Childs, L. C.; Meng, Shi-Yuan; Bennett, George N.

doi:10.1111/j.1365-2958.1989.tb00208.x

Cited by 96 publications

(74 citation statements)

References 51 publications

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“…Conceivably, coordinate regulation of the synthesis of the precursor/ product antiporter with the decarboxylase minimizes excessive precursor and/or product accumulation in the cells. In this regard it is tempting to suggest that synthesis of these antiporters, like expression of the genes that encode the corresponding decarboxylases, is induced at low external pH and/or during oxygen limitation (Gale, 1946;Auger et al, 1989;Gamper et al, 1991;Watson et al, 1992). Since this manuscript was completed, three new members of the APC family have been identified.…”

Section: <Smentioning

confidence: 99%

Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria

et al. 1993

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We demonstrate that three integral membrane receptors of mammals-the ecotropic retroviral leukemia receptor (ERR), the human retroviral receptor (HRR), and the T-cell early activator (Tea)-are homologous to a family of transporters specific for amino acids, polyamines, and choline (APC), which catalyze solute uniport, so1ute:cation symport, or so1ute:solute antiport in yeast, fungi, and eubacteria. Interestingly, the ERR membrane protein was recently shown to function as a cation:amino acid cotransporter. A binary sequence similarity matrix and an evolutionary tree of the 14 members of this family, illustrating their sequence similarities and divergences, were constructed. Other proteins, including the developmentally controlled GerAII spore germination protein of Bacillus subtilis and the acetylcho~ine receptor of D r~s o~~i l a ~e I a n o~a s t e r gave sequence comparison scores of a sufficiently large magnitude to suggest (but not to establish) a common evolutionary origin with members of the APC family.We report an extended and corrected Tea cDNA sequence and show that the mammalian Tea and ERR encoding genes are differentially expressed in tissues and cell lines. Furthermore, the two mammalian cDNA sequences hybridize with other vertebrate and yeast genomic DNAs under stringent conditions. These observations support the notion that cell surface receptor proteins in mammals are transport proteins that share a common origin with transport proteins of single-ceiled organisms. Thus, permeases of essential metabolites may function pathologically as viral receptors.

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Section: <Smentioning

confidence: 99%

Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria

et al. 1993

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“…First, to maintain pH homeostasis under mild acid shock, bacteria induce a change in the composition of outer-membrane proteins and in cell-surface hydrophobicity (Dilworth & Glenn, 1999). Next or concomitantly, Gram-negative and Gram-positive bacteria induce mechanisms specifically associated with pH resistance such as those involved in the synthesis of degradative amino acid decarboxylases (Auger et al, 1989;Castanie-Cornet et al, 1999;Gale, 1946;Rescei & Snell, 1972;Tabor & Tabor, 1985).…”

Section: Introductionmentioning

confidence: 99%

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

et al. 2004

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In several Gram-positive and Gram-negative bacteria glutamate decarboxylases play an important role in the maintenance of cellular homeostasis in acid environments. Here, new insight is brought to the regulation of the acid response in Escherichia coli. Overexpression of yhiE, similarly to overexpression of gadX, a known regulator of glutamate decarboxylase expression, leads to increased resistance of E. coli strains under high acid conditions, suggesting that YhiE is a regulator of gene expression in the acid response. Target genes of both YhiE (renamed GadE) and GadX were identified by a transcriptomic approach. In vitro experiments with GadE purified protein provided evidence that this regulator binds to the promoter region of these target genes. Several of them are clustered together on the chromosome and this chromosomal organization is conserved in many E. coli strains. Detailed structural (in silico) analysis of this chromosomal region suggests that the promoters of the corresponding genes are preferentially denatured. These results, along with the G+C signature of the chromosomal region, support the existence of a fitness island for acid adaptation on the E. coli chromosome.

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“…The lysine decarboxylase CadA converts lysine upon consumption of a cytoplasmic proton to cadaverine and carbon dioxide. Subsequently, CadB transports the basic reaction product cadaverine in exchange for lysine out of the cell (2,3). Transcription of the cadBA operon in E. coli is activated when the external pH drops below pH 6.6 if external lysine is available (4,5).…”

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confidence: 99%

New Insights into the Signaling Mechanism of the pH-responsive, Membrane-integrated Transcriptional Activator CadC of Escherichia coli

Haneburger

Eichinger

Skerra

et al. 2011

Journal of Biological Chemistry

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The membrane-integrated transcriptional regulator CadC of Escherichia coli activates expression of the cadBA operon at low external pH with concomitantly available lysine, providing adaptation to mild acidic stress. CadC is a representative of the ToxR-like proteins that combine sensory, signal transduction, and DNA-binding activities within a single polypeptide. Although several ToxR-like regulators such as CadC, as well as the main regulator of Vibrio cholerae virulence, ToxR itself, which activate gene expression at acidic pH, have been intensively investigated, their molecular activation mechanism is still unclear. In this study, a structure-guided mutational analysis was performed to elucidate the mechanism by which CadC detects acidification of the external milieu. Thus, a cluster of negatively charged amino acids (Asp-198, Asp-200, Glu-461, Glu-468, and Asp-471) was found to be crucial for pH detection. These amino acids form a negatively charged patch on the surface of the periplasmic domain of CadC that stretches across its two subdomains. The results of different combinations of amino acid replacements within this patch indicated that the N-terminal subdomain integrates and transduces the signals coming from both subdomains to the transmembrane domain. Alterations in the phospholipid composition did not influence pH-dependent cadBA expression, and therefore, interplay of the acidic surface patch with the negatively charged headgroups is unlikely. Models are discussed according to which protonation of these acidic amino acid side chains reduces repulsive forces between the two subdomains and/or between two monomers within a CadC dimer and thereby enables receptor activation upon lowering of the environmental pH.

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Construction of lac fusions to the inducible arginine‐and lysine decarboxylase genes of Escherichia coli K12

Cited by 96 publications

References 51 publications

Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria

Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

New Insights into the Signaling Mechanism of the pH-responsive, Membrane-integrated Transcriptional Activator CadC of Escherichia coli

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