Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase.
AUTOR(ES)
Arnau, J
RESUMO
The Lactococcus lactis pfl gene, encoding pyruvate formate-lyase (PFL), has been cloned and characterized. The deduced amino acid sequence of the L. lactis PFL. protein showed high similarity to those of other bacterial PFL proteins and included the conserved glycine residue involved in posttranslational activation of PFL. The genetic organization of the chromosomal pfl region in L. lactis showed differences from other characterized pfl loci, with an upstream open reading frame independently transcribed in the same orientation as the pfl gene. The gene coding for PFL-activase (act), normally found downstream of pfl, was not identified in L. lactis. Analysis of pfl expression showed a strong induction under anaerobiosis at the transcriptional level independent of the growth medium used. During growth with galactose, pfl showed the highest levels of expression. Constructed L. lactis pfl strains were unable to produce formate under anaerobic growth. Higher levels of diacetyl and acetoin were produced anaerobically in the constructed Lactococcus lactis subsp. lactis biovar diacetylactis pfl strain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=179481Documentos Relacionados
- Cloning and sequence analysis of the pfl gene encoding pyruvate formate-lyase from Streptococcus mutans.
- Synthesis and Posttranslational Regulation of Pyruvate Formate-Lyase in Lactococcus lactis
- Carbon metabolism regulates expression of the pfl (pyruvate formate-lyase) gene in Escherichia coli.
- Post-translational activation introduces a free radical into pyruvate formate-lyase.
- Characterization of the Streptococcus mutans Pyruvate Formate-Lyase (PFL)-Activating Enzyme Gene by Complementary Reconstitution of the In Vitro PFL-Reactivating System