Nitrogen regulation in bacteria and archaea

Annu Rev Microbiol. 2007;61:349-77. doi: 10.1146/annurev.micro.61.080706.093409.

Abstract

A wide range of Bacteria and Archaea sense cellular 2-oxoglutarate (2OG) as an indicator of nitrogen limitation. 2OG sensor proteins are varied, but most of those studied belong to the PII superfamily. Within the PII superfamily, GlnB and GlnK represent a widespread family of homotrimeric proteins (GlnB-K) that bind and respond to 2OG and ATP. In some bacterial phyla, GlnB-K proteins are covalently modified, depending on enzymes that sense cellular glutamine as an indicator of nitrogen sufficiency. GlnB-K proteins are central clearing houses of nitrogen information and bind and modulate a variety of nitrogen assimilation regulators and enzymes. NifI(1) and NifI(2) comprise a second widespread family of PII proteins (NifI) that are heteromultimeric, respond to 2OG and ATP, and bind and regulate dinitrogenase in Euryarchaeota and many Bacteria.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Alphaproteobacteria / metabolism
  • Archaea / metabolism*
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology
  • Cyanobacteria / metabolism
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology
  • Glutamate-Ammonia Ligase / genetics
  • Nitrogen / metabolism*
  • Nucleotidyltransferases / chemistry
  • Nucleotidyltransferases / physiology
  • PII Nitrogen Regulatory Proteins / chemistry
  • PII Nitrogen Regulatory Proteins / physiology
  • Phylogeny
  • Signal Transduction

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • PII Nitrogen Regulatory Proteins
  • PIID regulatory protein, Bacteria
  • glnK protein, E coli
  • Nucleotidyltransferases
  • Glutamate-Ammonia Ligase
  • Nitrogen