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Sensory components controlling bacterial nitrogen assimilation

E S Kamberov1, M R Atkinson, J Feng

  • 1Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606.

Cellular & Molecular Biology Research
|January 1, 1994
PubMed
Summary
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The PII protein in enteric bacteria regulates nitrogen assimilation (Ntr regulon) by modulating the activity of NRII and NRI proteins. This study clarifies PII

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Enteric bacteria utilize the Ntr regulon for nitrogen assimilation, controlled by a complex signal transduction system.
  • Key components include uridylyltransferase/uridylyl-removing enzyme (UTase/UR), PII protein, NRII (kinase/phosphatase), and NRI (transcription factor).
  • PII protein's role in regulating Ntr transcription via NRII's phosphatase activity is partially understood.

Purpose of the Study:

  • To refine purification and assay methods for UTase/UR and PII proteins.
  • To investigate the precise mechanism by which PII influences the NRII-NRI signaling cascade.
  • To characterize the PII-dependent regulated phosphatase activity.

Main Methods:

  • Improved purification protocols for UTase/UR and PII proteins.

Related Experiment Videos

  • Crystallization of the PII protein.
  • Enzyme activity assays for UTase/UR and PII, focusing on NRII and NRI interactions.

    • Main Results:

    • Purified PII protein effectively elicits the regulated phosphatase activity.
    • PII does not influence NRII autophosphorylation or phosphoryl group transfer to NRI.
    • Regulated phosphatase activity is highly dependent on the ratio of phosphorylated NRI (NRI approximately P) to unphosphorylated NRI, and acts on the N-terminal domain of NRI.

    Conclusions:

    • PII's primary role is to activate the dephosphorylation of NRI approximately P, rather than affecting NRII's kinase activity.
    • The regulation of Ntr transcription is finely tuned by the PII-mediated modulation of NRI approximately P levels.
    • This study provides a clearer mechanistic understanding of nitrogen signal transduction in enteric bacteria.