Abstract
The PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942 signals the cellular N status by being phosphorylated or dephosphorylated at a seryl residue. Here we show that the PII-modifying system responds to the activity of ammonium assimilation via the glutamine synthase-glutamate synthase pathway and to the state of CO2 fixation. To identify possible functions of PII in this microorganism, a PII-deficient mutant was created and its general phenotype was characterized. The analysis shows that the PII protein interferes with the regulation of enzymes required for nitrogen assimilation, although ammonium repression is still detectable in the PII-deficient mutant. We suggest that the phosphorylation and dephosphorylation of PII are part of a complex signal transduction network involved in global nitrogen control in cyanobacteria. In this regulatory process, PII might be involved in mediating the tight coordination between carbon and nitrogen assimilation.
MeSH Terms
Bacterial Proteins/genetics,metabolism
Biological Transport, Active
Carbon/metabolism
Carbon Dioxide/metabolism
Chromosome Mapping
Cyanobacteria/genetics,metabolism
Genes, Bacterial
Glutamate-Ammonia Ligase/metabolism
Methylamines/metabolism
Mutation
Nitrate Reductase
Nitrate Reductases/metabolism
Nitrite Reductases/metabolism
Nitrogen/metabolism
PII Nitrogen Regulatory Proteins
Phenotype
Phosphorylation
Signal Transduction/genetics,physiology
Chemicals
Bacterial Proteins
Methylamines
PII Nitrogen Regulatory Proteins
Carbon Dioxide
PIID regulatory protein, Bacteria
Carbon
methylamine
Nitrate Reductases
Nitrite Reductases
Nitrate Reductase
Glutamate-Ammonia Ligase
Nitrogen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Forchhammer K
Département de Biochimie et Génétique Moléculaire, Institut Pasteur, Paris, France.
Tandeau de Marsac N
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