scholarly journals Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli

2013 ◽  
Vol 1827 (8-9) ◽  
pp. 1086-1101 ◽  
Author(s):  
Chantal Iobbi-Nivol ◽  
Silke Leimkühler
Keyword(s):  
Escherichia Coli ◽  
Molybdenum Cofactor ◽  
Molybdenum Enzymes ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals Crystal Structure of the Molybdenum Cofactor Biosynthesis Protein MobA from Escherichia coli at Near-Atomic Resolution

Structure ◽  
2000 ◽  
Vol 8 (11) ◽  
pp. 1115-1125 ◽  
Author(s):  
Clare E.M. Stevenson ◽  
Frank Sargent ◽  
Grant Buchanan ◽  
Tracy Palmer ◽  
David M. Lawson
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Molybdenum Cofactor ◽  
Atomic Resolution ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

scholarly journals Chlamydomonas reinhardtii CNX1E Reconstitutes Molybdenum Cofactor Biosynthesis in Escherichia coli Mutants

2007 ◽  
Vol 6 (6) ◽  
pp. 1063-1067 ◽  
Author(s):  
Ángel Llamas ◽  
Manuel Tejada-Jimenez ◽  
David González-Ballester ◽  
José Javier Higuera ◽  
Guenter Schwarz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Chlamydomonas Reinhardtii ◽  
Double Mutant ◽  
Molybdenum Cofactor ◽  
Wild Type ◽  
Eukaryotic Protein ◽  
E Coli ◽  
Wild Type Phenotype ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis

ABSTRACT We have isolated and characterized the Chlamydomonas reinhardtii genes for molybdenum cofactor biosynthesis, namely, CNX1G and CNX1E, and expressed them and their chimeric fusions in Chlamydomonas and Escherichia coli. In all cases, the wild-type phenotype was restored in individual mutants as well as in a CNX1G CNX1E double mutant. Therefore, CrCNX1E is the first eukaryotic protein able to complement an E. coli moeA mutant.

scholarly journals Hypersensitivity of Escherichia coli Δ(uvrB-bio) Mutants to 6-Hydroxylaminopurine and Other Base Analogs Is Due to a Defect in Molybdenum Cofactor Biosynthesis

2000 ◽  
Vol 182 (12) ◽  
pp. 3361-3367 ◽  
Author(s):  
Stanislav G. Kozmin ◽  
Youri I. Pavlov ◽  
Ronnie L. Dunn ◽  
Roel M. Schaaper
Keyword(s):  
Escherichia Coli ◽  
Point Mutation ◽  
Excision Repair ◽  
Molybdenum Cofactor ◽  
Transposon Insertion ◽  
Serovar Typhimurium ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis ◽  
Repair Defect ◽  
Related Compounds

ABSTRACT We have shown previously that Escherichia coli andSalmonella enterica serovar Typhimurium strains carrying a deletion of the uvrB-bio region are hypersensitive to the mutagenic and toxic action of 6-hydroxylaminopurine (HAP) and related base analogs. This sensitivity is not due to theuvrB excision repair defect associated with this deletion because a uvrB point mutation or a uvrAdeficiency does not cause hypersensitivity. In the present work, we have investigated which gene(s) within the deleted region may be responsible for this effect. Using independent approaches, we isolated both a point mutation and a transposon insertion in themoeA gene, which is located in the region covered by the deletion, that conferred HAP sensitivity equal to that conferred by theuvrB-bio deletion. The moeAB operon provides one of a large number of genes responsible for biosynthesis of the molybdenum cofactor. Defects in other genes in the same pathway, such as moa or mod, also lead to the same HAP-hypersensitive phenotype. We propose that the molybdenum cofactor is required as a cofactor for an as yet unidentified enzyme (or enzymes) that acts to inactivate HAP and other related compounds.

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