A Corynebacterium glutamicum mutant with a defined deletion within the rplk gene is impaired in (p)ppGpp accumulation upon amino acid starvation
Article Abstract:
The mutant of Corynebacterium glutamicum, which carries a 12 base pair in-frame deletion within rplk gene, fails to accumulate the hyperphosphorylated guanosine nucleotides in an adaptational response to amino acid starvation. The mutant shows increased tolerance to thiostrepton antibiotic.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
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Allophane increases the protein levels of several cephamycin biosynthetic enzymes in Nocardia lactamdurans
Article Abstract:
Increased activities and/or an extended life in the cell of four cephamycin biosynthetic enzymes were noted in allophane-supplemented cultures. These enzymes are isopenicillin N synthase, the two-protein-component 7(alpha)-cephem methoxylase and 3'-hydroxymethylcephem O-carbamoyltransferase. Allophane-supplemented cultures also showed increased protein levels of alpha-aminoadipyl-cysteinyl-valine synthetase and the two proteins involved in the 7(alpha)-cephem methoxylase. This was gleaned from a study of the effect of the addition of allophane to two different strains of N. lactamdurans on cephamycin biosynthesis. Allophane was found to reverse the inhibitory effect of inorganic phosphate on the biosynthesis of cephamycin.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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The role of the Corynebacterium glutamicum rel gene in (p)ppGpp metabolism
Article Abstract:
A PCR-based approach was used to examine the (p)ppGpp metabolism of amino-acid-producing coryneform bacteria. This method required the isolation of the rel gene of Corynebacterium glutamicum ATCC 13032. Results revealed similarities between the amino acid sequence and the RelA and SpoT proteins of Escherichia coli. The rel gene was found to exhibit bifunctional capabilities as seen from the encoding of both (p)ppGpp synthetase and (p)ppGpp-degrading activities.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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