The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels
1 Department of Biochemistry, Medical Sciences Institute, Dundee University, Dundee DD1 4HN, UK ABSTRACT Summary: The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from molybdopterin and GTP. Reporter t...
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Published in | Microbiology (Society for General Microbiology) Vol. 141; no. 7; pp. 1663 - 1671 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Soc General Microbiol
01.07.1995
Society for General Microbiology |
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Abstract | 1 Department of Biochemistry, Medical Sciences Institute, Dundee University, Dundee DD1 4HN, UK
ABSTRACT
Summary: The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from molybdopterin and GTP. Reporter translational lac fusion mutations in the mobA gene have been constructed using plac Mu9 mutagenesis. The mob locus is expressed at very low levels under both aerobic and anaerobic growth conditions. Neither additions to the growth media (nitrate, tungstate or molybdate) nor secondary mutations at the moa, mob, mod, moe or mog loci affected the level of expression. Two transcription initiation sites and their associated promoter regions have been identified upstream of mobA . Both of the promoter regions show a poor match to the –35 and –10 consensus sequences for –70 promoters. A 2-2 kb chromosomal DNA fragment which complemented all available mob mutants has been sequenced. Two ORFs were identified, arranged as a single transcription unit. The encoded polypeptides have predicted molecular masses of 21642 Da and 19362 Da, respectively. The DNA has been subcloned into a T7 overexpression system and the predicted products identified. The mobA gene encodes protein FA, which has been purified to homogeneity and brings about the activation of inactive molybdoenzymes in cell extracts of mob mutants. The mobB gene encodes a polypeptide with a putative nucleotide binding site. All available mob mutations which have been selected for by their ability to grow anaerobically in the presence of chlorate are located in the mobA gene.
2 Author for correspondence: David H. Boxer. Tel: +44 1382 344880. Fax: +44 1382 322558 e-mail: dhboxer@ bad.dundee.ac.uk
Keywords: Escherichia coli K12, mob locus, molybdenum cofactor biosynthesis, molybdopterin guanine dinucleotide
Present address: Laboratoire de Chimie Bacterienne, CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille, Cedex 9, France. |
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AbstractList | 1 Department of Biochemistry, Medical Sciences Institute, Dundee University, Dundee DD1 4HN, UK
ABSTRACT
Summary: The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from molybdopterin and GTP. Reporter translational lac fusion mutations in the mobA gene have been constructed using plac Mu9 mutagenesis. The mob locus is expressed at very low levels under both aerobic and anaerobic growth conditions. Neither additions to the growth media (nitrate, tungstate or molybdate) nor secondary mutations at the moa, mob, mod, moe or mog loci affected the level of expression. Two transcription initiation sites and their associated promoter regions have been identified upstream of mobA . Both of the promoter regions show a poor match to the –35 and –10 consensus sequences for –70 promoters. A 2-2 kb chromosomal DNA fragment which complemented all available mob mutants has been sequenced. Two ORFs were identified, arranged as a single transcription unit. The encoded polypeptides have predicted molecular masses of 21642 Da and 19362 Da, respectively. The DNA has been subcloned into a T7 overexpression system and the predicted products identified. The mobA gene encodes protein FA, which has been purified to homogeneity and brings about the activation of inactive molybdoenzymes in cell extracts of mob mutants. The mobB gene encodes a polypeptide with a putative nucleotide binding site. All available mob mutations which have been selected for by their ability to grow anaerobically in the presence of chlorate are located in the mobA gene.
2 Author for correspondence: David H. Boxer. Tel: +44 1382 344880. Fax: +44 1382 322558 e-mail: dhboxer@ bad.dundee.ac.uk
Keywords: Escherichia coli K12, mob locus, molybdenum cofactor biosynthesis, molybdopterin guanine dinucleotide
Present address: Laboratoire de Chimie Bacterienne, CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille, Cedex 9, France. The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from molybdopterin and GTP. Reporter translational lac fusion mutations in the mobA gene have been constructed using lambda placMu9 mutagenesis. The mob locus is expressed at very low levels under both aerobic and anaerobic growth conditions. Neither additions to the growth media (nitrate, tungstate or molybdate) nor secondary mutations at the moa, mob, mod, moe or mog loci affected the level of expression. Two transcription initiation sites and their associated promoter regions have been identified upstream of mobA. Both of the promoter regions show a poor match to the -35 and -10 consensus sequences for sigma super(70) promoters. A 2.2 kb chromosomal DNA fragment which complemented all available mob mutants has been sequenced. Two ORFs were identified, arranged as a single transcription unit. The encoded polypeptides have predicted molecular masses of 21642 Da and 19362 Da, respectively. The DNA has been subcloned into a T7 overexpression system and the predicted products identified. The mobA gene encodes protein FA, which has been purified to homogeneity and brings about the activation of inactive molybdoenzymes in cell extracts of mob mutants. The mobB gene encodes a polypeptide with a putative nucleotide binding site. All available mob mutations which have been selected for by their ability to grow anaerobically in the presence of chlorate are located in the mobA gene. The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from molybdopterin and GTP. Reporter translational lac fusion mutations in the mobA gene have been constructed using lambda placMu9 mutagenesis. The mob locus is expressed at very low levels under both aerobic and anaerobic growth conditions. Neither additions to the growth media (nitrate, tungstate or molybdate) nor secondary mutations at the moa, mob, mod, moe or mog loci affected the level of expression. Two transcription initiation sites and their associated promoter regions have been identified upstream of mobA. Both of the promoter regions show a poor match to the -35 and -10 consensus sequences for sigma 70 promoters. A 2.2 kb chromosomal DNA fragment which complemented all available mob mutants has been sequenced. Two ORFs were identified, arranged as a single transcription unit. The encoded polypeptides have predicted molecular masses of 21642 Da and 19362 Da, respectively. The DNA has been subcloned into a T7 overexpression system and the predicted products identified. The mobA gene encodes protein FA, which has been purified to homogeneity and brings about the activation of inactive molybdoenzymes in cell extracts of mob mutants. The mobB gene encodes a polypeptide with a putative nucleotide binding site. All available mob mutations which have been selected for by their ability to grow anaerobically in the presence of chlorate are located in the mobA gene. |
Author | Boxer, David H lobbi-Nivol, Chantal Palmer, Tracy McNairn, Elizabeth Whitty, Patrick W |
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Keywords | Gene Nucleotide sequence Transcription Escherichia coli Bacteria Biosynthesis Gene expression Cofactor Molybdenum Aminoacid sequence Enterobacteriaceae |
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Snippet | 1 Department of Biochemistry, Medical Sciences Institute, Dundee University, Dundee DD1 4HN, UK
ABSTRACT
Summary: The mob locus of Escherichia coli encodes... The mob locus of Escherichia coli encodes functions which catalyse the synthesis of active molybdenum cofactor, molybdopterin guanine dinucleotide, from... |
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SubjectTerms | Amino Acid Sequence Anaerobiosis Bacterial Proteins - biosynthesis Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacteriology Base Sequence Biological and medical sciences Chlorates - pharmacology Cloning, Molecular Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Genes, Bacterial Genetics Guanine Nucleotides - biosynthesis Guanine Nucleotides - genetics Guanine Nucleotides - metabolism Microbiology Molecular Sequence Data Mutagenesis, Insertional Nitrate Reductases - genetics Operon Peptide Elongation Factor Tu - genetics Promoter Regions, Genetic Pterins - metabolism Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - metabolism Restriction Mapping Sequence Homology, Amino Acid Transduction, Genetic |
Title | The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels |
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