An additional PII in Escherichia coli: a new regulatory protein in the glutamine synthetase cascade

FEMS Microbiol Lett. 1995 Oct 1;132(1-2):153-7. doi: 10.1111/j.1574-6968.1995.tb07825.x.

Abstract

The PII protein in the glutamine synthetase cascade transduces the nitrogen signal, as sensed by uridylyltransferase, both to the NRII/NRI two-component system and to adenylyltransferase, to regulate the activity of glutamine synthetase. Here we describe the amplification of a chromosomal DNA fragment from Escherichia coli which contains the sequence of a PII homologue. The derived amino acid sequence of this DNA fragment is 67% identical to E. coli PII. It contains the conserved tyrosine residue which is known to be the site of uridylylation in PII. E. coli is the first organism in which two different PII proteins have been detected.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • DNA, Bacterial
  • Enzyme Induction
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Gene Amplification
  • Glutamate-Ammonia Ligase / genetics*
  • Glutamate-Ammonia Ligase / metabolism
  • Molecular Sequence Data
  • Nitrogen / metabolism
  • PII Nitrogen Regulatory Proteins
  • Protein Kinases / genetics*
  • Protein Kinases / isolation & purification
  • Protein Kinases / metabolism
  • Sequence Homology
  • Signal Transduction
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • PII Nitrogen Regulatory Proteins
  • Transcription Factors
  • glnG protein, E coli
  • PIID regulatory protein, Bacteria
  • Protein Kinases
  • Glutamate-Ammonia Ligase
  • Nitrogen

Associated data

  • GENBANK/S79842
  • GENBANK/U40429