Mutations in sdh (succinate dehydrogenase genes) alter the thiamine requirement of Salmonella typhimurium.
AUTOR(ES)
Enos-Berlage, J L
RESUMO
Mutants lacking the first enzyme in de novo purine synthesis (PurF) can synthesize thiamine if increased levels of pantothenate are present in the culture medium (J. L. Enos-Berlage and D. M. Downs, J. Bacteriol. 178:1476-1479, 1996). Derivatives of purF mutants that no longer required pantothenate for thiamine-independent growth were isolated. Analysis of these mutants demonstrated that they were defective in succinate dehydrogenase (Sdh), an enzyme of the tricarboxylic acid cycle. Results of phenotypic analyses suggested that a defect in Sdh decreased the thiamine requirement of Salmonella typhimurium. This reduced requirement correlated with levels of succinyl-coenzyme A (succinyl-CoA), which is synthesized in a thiamine pyrophosphate-dependent reaction. The effect of succinyl-CoA on thiamine metabolism was distinct from the role of pantothenate in thiamine synthesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=179209Documentos Relacionados
- Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium.
- Thiamine pyrophosphate (TPP) negatively regulates transcription of some thi genes of Salmonella typhimurium.
- Involvement of the oxidative pentose phosphate pathway in thiamine biosynthesis in Salmonella typhimurium.
- Mutations in trans that affect formate dehydrogenase (fdhF) gene expression in Salmonella typhimurium.
- Mutations in rpoA affect expression of anaerobically regulated genes in Salmonella typhimurium.