Role of the dsdC activator in regulation of D-serine deaminase synthesis.
The activator of the D-serine deaminase operon, the product of the dsdC gene, has been partially purified. It is reasonably stable to routine purification procedures in the presence of its ligand D-serine, but not in its absence. It loses activity upon dialysis in amino acid-free buffer, but activity is completely restored upon readdition of D-serine. It apparently functions purely as an activator, no repressor function could be demonstrated at suboptimal D-serine concentration. It is a transcriptional control element. The time required for in vitro transcription of D-serine deaminase mRNA, nearly 4 min, is similar to that for beta-galactosidase. Since the beta-galactosidase monomer is a much protein, this is surprisingly long.
D001426:Bacterial Proteins / Q000502:physiology*; D004265:DNA Helicases / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005809:Genes, Regulator; D012695:L-Serine Dehydratase / Q000096:biosynthesis*; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000096:biosynthesis; D012333:RNA, Messenger / Q000096:biosynthesis; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; D004265:DNA Helicases; D012695:L-Serine Dehydratase