Sequence, transcriptional, and functional analyses of the valine (branched-chain amino acid) dehydrogenase gene of Streptomyces coelicolor.
AUTOR(ES)
Tang, L
RESUMO
The gene encoding the valine (branched-chain amino acid) dehydrogenase (Vdh) from Streptomyces coelicolor has been characterized as follows. The vdh gene was identified by hybridization to a specific oligodeoxynucleotide that was synthesized on the basis of the N-terminal amino acid sequence of purified Vdh. Nucleotide sequence analysis predicts that the vdh gene contains a 364-amino-acid open reading frame that should produce a 38,305-M(r) protein. The deduced amino acid sequence of the Vdh protein is significantly similar to those of several other amino acid dehydrogenases, especially the leucine and phenylalanine dehydrogenases from Bacillus spp. The vdh gene is apparently transcribed from a single major transcriptional start point, separated by only 8 bp from the 5' end of a divergent transcript and located 63 bp upstream from the vdh translational start point. Mutants with a disrupted vdh gene have no detectable Vdh activity and have lost the ability to grow on valine, leucine, or isoleucine as the sole nitrogen source. This vdh mutation does not significantly affect growth or actinorhodin production in a minimal medium, yet the addition of 0.2% L-valine to the medium provokes approximately 32 and 80% increases in actinorhodin production in vdh+ and vdh strains, respectively.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=204847Documentos Relacionados
- The bkdR Gene of Streptomyces coelicolor Is Required for Morphogenesis and Antibiotic Production and Encodes a Transcriptional Regulator of a Branched-Chain Amino Acid Dehydrogenase Complex
- Transcriptional Organization and Posttranscriptional Regulation of the Bacillus subtilis Branched-Chain Amino Acid Biosynthesis Genes
- Cloning and characterization of a gene (msdA) encoding methylmalonic acid semialdehyde dehydrogenase from Streptomyces coelicolor.
- Gene inactivation in Lactococcus lactis: branched-chain amino acid biosynthesis.
- Transcriptional analysis of the promoter region of the Pseudomonas putida branched-chain keto acid dehydrogenase operon.