Inducer expulsion and the occurrence of an HPr(Ser-P)-activated sugar-phosphate phosphatase in Enterococcus faecalis and Streptococcus pyogenes

Article Abstract:

Inducer expulsion refers to the phenomenon wherein adding a metabolizable carbohydrate to a microorganism's growth medium leads to the rapid efflux of pre-accumulated sugar-phosphates. Past studies have shown that this phenomenon occurs in Streptococcus pyogenes, Streptococcus bovis and Lactococcus lactics. It is shown that inducer expulsion also occurs in Enterococcus faecalis as a result of the action of the metabolite-activated ATP-dependent HPr(Ser) kinase, the same kinase which governs the occurrence of the phenomenon in Streptococcus pyogenes.

Bacteria, Streptococcus pyogenes, Carbohydrate metabolism

---

A hybrid response regulator possessing a PEP-dependent phosphorylation domain

Article Abstract:

A unique modular multidomain protein from Clostridium acetobutylicum was characterized. It supported elements determined from the photransferase system (PTS) and response regulators. It also exhibited sequence similarity with the NtrC family of response regulators in its two C-terminal domains. In addition, a HPr-response regulator was described to promote an example of a transcriptional regulator phosphorylated by the PTS.

Proteins, Phosphorylation

---

Similar abstracts:

• Abstracts: Identification of an alternative 2,3-dihydroxybiphenyl 1,2-dioxygenase in Rhodococcus sp. strain RHA1 and cloning of the gene
• Abstracts: Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
• Abstracts: Determinants of regulated proteolysis in signal transduction. Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease
• Abstracts: A Bacillus subtilis gene cluster similar to the Escherichia coli phosphate-specific transport (pst) operon: evidence for a tandemly arranged pstB gene
• Abstracts: Stat3 as an oncogene. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.