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Literature summary for 1.18.6.1 extracted from
- How posttranslational modification of nitrogenase is circumvented in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively (2012), Appl. Environ. Microbiol., 78, 1023-1032.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodopseudomonas palustris | - |
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General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | posttranslational regulation of nitrogenase activity in Rhodopseudomonas palustris depends on proteins DraT2, an ADP-ribosyltransferase, and GlnK2, an NtrC-regulated PII protein. GlnK2 is not well expressed in ammonium-grown NifA mutant cells that express nitrogenase genes constitutively and produce H2 when grown with ammonium as a nitrogen source. The mutant strain has elevated nitrogenase activity due to overexpression of the nif genes, and this increased amount of expression overwhelms a basal level of activity of DraT2 in ammonium-grown cells. Insufficient levels of both GlnK2 and DraT2 allow H2 production by an nifA* mutant grown with ammonium. Inactivation of the nitrogenase posttranslational modification system by mutation of draT2 results in increased H2 production by the ammonium-grown mutant cells | Rhodopseudomonas palustris |
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