author_facet Wendrich, Thomas M.
Marahiel, Mohamed A.
Wendrich, Thomas M.
Marahiel, Mohamed A.
author Wendrich, Thomas M.
Marahiel, Mohamed A.
spellingShingle Wendrich, Thomas M.
Marahiel, Mohamed A.
Molecular Microbiology
Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
Molecular Biology
Microbiology
author_sort wendrich, thomas m.
spelling Wendrich, Thomas M. Marahiel, Mohamed A. 0950-382X 1365-2958 Wiley Molecular Biology Microbiology http://dx.doi.org/10.1046/j.1365-2958.1997.5511919.x <jats:p>A PCR‐amplified DNA fragment of the <jats:italic>relA</jats:italic> gene from genomic <jats:italic>Bacillus subtilis</jats:italic> DNA was used to isolate the entire <jats:italic>relA</jats:italic>/<jats:italic>spoT</jats:italic> homologue and two adjacent open reading frames (ORFs) from a λ ZAP Express library. The <jats:italic>relA</jats:italic> gene, which encodes a protein of 734 amino acid residues (aa), is flanked by an ORF (170 aa) that shares high similarity to adenine phosphoribosyltransferase genes (<jats:italic>apt</jats:italic>), and downstream by an ORF (131 aa) of unknown function. This genetic organization is similar to that in <jats:italic>Streptomyces coelicolor</jats:italic> A3(2) and <jats:italic>Streptococcus equismilis</jats:italic> H46A. <jats:italic>relA</jats:italic> shows significant similarity to the <jats:italic>Escherichia coli relA</jats:italic> and <jats:italic>spoT</jats:italic> genes, which are responsible for the synthesis and degradation of the highly phosphorylated guanosine nucleotides (p)ppGpp, triggering the stringent response. Deletion of the <jats:italic>relA</jats:italic> gene generated a (p)ppGpp<jats:sup>0</jats:sup> phenotype that demonstrated its essential role in the response to amino acid deprivation and resulted in impaired/lowered induction of proteins involved in stress response as well as amino acid biosynthesis, as judged by two‐dimensional gel electrophoresis. The same effects of impaired induction of some σ<jats:sup>B</jats:sup>‐independent proteins could also be shown in a <jats:italic>sigB/relA</jats:italic> double mutant, supporting the role of <jats:italic>relA</jats:italic> in derepression/induction of catabolic and anabolic genes during stringent response.</jats:p> Cloning and characterization of a <i>relA</i>/<i>spoT</i> homologue from <i>Bacillus subtilis</i> Molecular Microbiology
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source_id 49
title Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_unstemmed Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_full Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_fullStr Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_full_unstemmed Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_short Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_sort cloning and characterization of a <i>rela</i>/<i>spot</i> homologue from <i>bacillus subtilis</i>
topic Molecular Biology
Microbiology
url http://dx.doi.org/10.1046/j.1365-2958.1997.5511919.x
publishDate 1997
physical 65-79
description <jats:p>A PCR‐amplified DNA fragment of the <jats:italic>relA</jats:italic> gene from genomic <jats:italic>Bacillus subtilis</jats:italic> DNA was used to isolate the entire <jats:italic>relA</jats:italic>/<jats:italic>spoT</jats:italic> homologue and two adjacent open reading frames (ORFs) from a λ ZAP Express library. The <jats:italic>relA</jats:italic> gene, which encodes a protein of 734 amino acid residues (aa), is flanked by an ORF (170 aa) that shares high similarity to adenine phosphoribosyltransferase genes (<jats:italic>apt</jats:italic>), and downstream by an ORF (131 aa) of unknown function. This genetic organization is similar to that in <jats:italic>Streptomyces coelicolor</jats:italic> A3(2) and <jats:italic>Streptococcus equismilis</jats:italic> H46A. <jats:italic>relA</jats:italic> shows significant similarity to the <jats:italic>Escherichia coli relA</jats:italic> and <jats:italic>spoT</jats:italic> genes, which are responsible for the synthesis and degradation of the highly phosphorylated guanosine nucleotides (p)ppGpp, triggering the stringent response. Deletion of the <jats:italic>relA</jats:italic> gene generated a (p)ppGpp<jats:sup>0</jats:sup> phenotype that demonstrated its essential role in the response to amino acid deprivation and resulted in impaired/lowered induction of proteins involved in stress response as well as amino acid biosynthesis, as judged by two‐dimensional gel electrophoresis. The same effects of impaired induction of some σ<jats:sup>B</jats:sup>‐independent proteins could also be shown in a <jats:italic>sigB/relA</jats:italic> double mutant, supporting the role of <jats:italic>relA</jats:italic> in derepression/induction of catabolic and anabolic genes during stringent response.</jats:p>
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author Wendrich, Thomas M., Marahiel, Mohamed A.
author_facet Wendrich, Thomas M., Marahiel, Mohamed A., Wendrich, Thomas M., Marahiel, Mohamed A.
author_sort wendrich, thomas m.
container_issue 1
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container_title Molecular Microbiology
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description <jats:p>A PCR‐amplified DNA fragment of the <jats:italic>relA</jats:italic> gene from genomic <jats:italic>Bacillus subtilis</jats:italic> DNA was used to isolate the entire <jats:italic>relA</jats:italic>/<jats:italic>spoT</jats:italic> homologue and two adjacent open reading frames (ORFs) from a λ ZAP Express library. The <jats:italic>relA</jats:italic> gene, which encodes a protein of 734 amino acid residues (aa), is flanked by an ORF (170 aa) that shares high similarity to adenine phosphoribosyltransferase genes (<jats:italic>apt</jats:italic>), and downstream by an ORF (131 aa) of unknown function. This genetic organization is similar to that in <jats:italic>Streptomyces coelicolor</jats:italic> A3(2) and <jats:italic>Streptococcus equismilis</jats:italic> H46A. <jats:italic>relA</jats:italic> shows significant similarity to the <jats:italic>Escherichia coli relA</jats:italic> and <jats:italic>spoT</jats:italic> genes, which are responsible for the synthesis and degradation of the highly phosphorylated guanosine nucleotides (p)ppGpp, triggering the stringent response. Deletion of the <jats:italic>relA</jats:italic> gene generated a (p)ppGpp<jats:sup>0</jats:sup> phenotype that demonstrated its essential role in the response to amino acid deprivation and resulted in impaired/lowered induction of proteins involved in stress response as well as amino acid biosynthesis, as judged by two‐dimensional gel electrophoresis. The same effects of impaired induction of some σ<jats:sup>B</jats:sup>‐independent proteins could also be shown in a <jats:italic>sigB/relA</jats:italic> double mutant, supporting the role of <jats:italic>relA</jats:italic> in derepression/induction of catabolic and anabolic genes during stringent response.</jats:p>
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spelling Wendrich, Thomas M. Marahiel, Mohamed A. 0950-382X 1365-2958 Wiley Molecular Biology Microbiology http://dx.doi.org/10.1046/j.1365-2958.1997.5511919.x <jats:p>A PCR‐amplified DNA fragment of the <jats:italic>relA</jats:italic> gene from genomic <jats:italic>Bacillus subtilis</jats:italic> DNA was used to isolate the entire <jats:italic>relA</jats:italic>/<jats:italic>spoT</jats:italic> homologue and two adjacent open reading frames (ORFs) from a λ ZAP Express library. The <jats:italic>relA</jats:italic> gene, which encodes a protein of 734 amino acid residues (aa), is flanked by an ORF (170 aa) that shares high similarity to adenine phosphoribosyltransferase genes (<jats:italic>apt</jats:italic>), and downstream by an ORF (131 aa) of unknown function. This genetic organization is similar to that in <jats:italic>Streptomyces coelicolor</jats:italic> A3(2) and <jats:italic>Streptococcus equismilis</jats:italic> H46A. <jats:italic>relA</jats:italic> shows significant similarity to the <jats:italic>Escherichia coli relA</jats:italic> and <jats:italic>spoT</jats:italic> genes, which are responsible for the synthesis and degradation of the highly phosphorylated guanosine nucleotides (p)ppGpp, triggering the stringent response. Deletion of the <jats:italic>relA</jats:italic> gene generated a (p)ppGpp<jats:sup>0</jats:sup> phenotype that demonstrated its essential role in the response to amino acid deprivation and resulted in impaired/lowered induction of proteins involved in stress response as well as amino acid biosynthesis, as judged by two‐dimensional gel electrophoresis. The same effects of impaired induction of some σ<jats:sup>B</jats:sup>‐independent proteins could also be shown in a <jats:italic>sigB/relA</jats:italic> double mutant, supporting the role of <jats:italic>relA</jats:italic> in derepression/induction of catabolic and anabolic genes during stringent response.</jats:p> Cloning and characterization of a <i>relA</i>/<i>spoT</i> homologue from <i>Bacillus subtilis</i> Molecular Microbiology
spellingShingle Wendrich, Thomas M., Marahiel, Mohamed A., Molecular Microbiology, Cloning and characterization of a relA/spoT homologue from Bacillus subtilis, Molecular Biology, Microbiology
title Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_full Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_fullStr Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_full_unstemmed Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_short Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
title_sort cloning and characterization of a <i>rela</i>/<i>spot</i> homologue from <i>bacillus subtilis</i>
title_unstemmed Cloning and characterization of a relA/spoT homologue from Bacillus subtilis
topic Molecular Biology, Microbiology
url http://dx.doi.org/10.1046/j.1365-2958.1997.5511919.x