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Functional analysis of the phosphoprotein PII (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Forchhammer, Karl Marsac, Nicole Tandeau De |
| Copyright Year | 1995 |
| 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. |
| Starting Page | 1 |
| Ending Page | 5 |
| Page Count | 5 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://jb.asm.org/content/177/8/2033.full.pdf |
| PubMed reference number | 7721695v1 |
| Volume Number | 177 |
| Issue Number | 8 |
| Journal | Journal of bacteriology |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | CDISC SDTM Microorganism Terminology Carbon Dioxide Cyanobacteria Genome Encoded Entity Glutamate Synthase Glutamate-Ammonia Ligase Glutamic Acid Glutamine Phosphoproteins Protein dephosphorylation Protein phosphatase Regulation of biological process Repression, Psychology Signal Transduction Synechococcus ammonium lactate |
| Content Type | Text |
| Resource Type | Article |
