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The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis expressed at very low levels

Article Abstract:

A study of the construction of nine "mob" mutants of Escherichia coli by gamma-placMu9 mutagenesis in which the mob promoter controls the activity of beta-galactosidase shows that the mob is expressed at very low levels under anaerobic and aerobic growth conditions. The mob locus of Escherichia coli facilitates the synthesis of molybdoprotein guanine dinucleotide, a molybdenum cofactor from GTP and molybdopterin. The mob locus DNA sequence show that the DNA encodes two ORF's present as a single transcription unit with polypeptide products of 21642 Da and 19362 Da.

Author: Palmer, Tracy, Iobbi-Nivol, Chantal, Whitty, Patrick W., McNairn, Elizabeth, Boxer, David H.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Analysis, Escherichia coli, Biosynthesis

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Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus

Article Abstract:

A study was conducted to analyze four genes of the DMSO respiratory gene cluster of Rhodobacter capsulatus. DNA cloning was carried out using conventional techniques. Experimental results indicated that DorR is a response regulator and is needed for the expression of the dorCDA operon. Findings also showed that the intergenic region between dorR and dorC contains four putative binding sites for DorR but no binding site for FnR.

Author: McEwan, Alastair G., Shaw, Anthony L., Leimkuhler, Silke, Klipp, Werner, Hanson, Graeme R.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
DNA, Operons

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Characterization of a molybdenum cofactor biosynthetic gene cluster in Rhodobacter capsulatus which is specific for the biogenesis of dimethylsulfoxide reductase

Article Abstract:

A study was conducted to analyze the effect of a mutation in moaA on oxomolybdenum enzyme activity and describe the cellular localization of the DMSO polypeptide in the mutant. The Moco biosynthetic gene cluster of the phagemid pALS1 was sequenced using the dye terminator technique. Experimental results indicated a mature form of DMSO reductase in the periplasms and a precursor form in the cytoplasm.

Author: Palmer, Tracy, Lane, Ian, McEwan, Alastair G., Shaw, Anthony L., Hanson, Graeme R., Solomon, Peter S.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
Enzymes, Polypeptides

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Subjects list: Research, Molybdenum
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