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. 1978 Oct;136(1):96–103. doi: 10.1128/jb.136.1.96-103.1978

Role of the dsdC activator in regulation of D-serine deaminase synthesis.

M C Heincz, E McFall
PMCID: PMC218636  PMID: 213419

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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