Isolation of a mutation resulting in constitutive synthesis of L-fucose catabolic enzymes.
AUTOR(ES)
Bartkus, J M
RESUMO
A ribitol-positive transductant of Escherichia coli K-12, JM2112, was used to facilitate the isolation and identification of mutations affecting the L-fucose catabolic pathway. Analysis of L-fucose-negative mutants of JM2112 enabled us to confirm that L-fucose-1-phosphate is the apparent inducer of the fucose catabolic enzymes. Plating of an L-fuculokinase-negative mutant of JM2112 on D-arabinose yielded an isolate containing a second fucose mutation which resulted in the constitutive synthesis of L-fucose permease, isomerase, and kinase. This constitutive mutation differs from the constitutive mutation described by Chen et al. (J. Bacteriol. 159:725-729, 1984) in that it is tightly linked to the fucose genes and appears to be located in the gene believed to code for the positive activator of the L-fucose genes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=214487Documentos Relacionados
- Natural and altered induction of the L-fucose catabolic enzymes in Klebsiella aerogenes.
- Constitutive activation of L-fucose genes by an unlinked mutation in Escherichia coli.
- BACTERIAL DISSIMILATION OF l-FUCOSE AND l-RHAMNOSE
- Clustering of genes for L-fucose dissimilation by Escherichia coli.
- Cross-induction of the L-fucose system by L-rhamnose in Escherichia coli.