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Article

Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense.

Journal of bacteriology - 1 Jul 1996

de Zamaroczy M, Paquelin A, Peltre G, Forchhammer K, Elmerich C

Abstract excerpt

The coexistence of two different PII, proteins in Azospirillum brasilense was established by comparing proteins synthesized by the wild-type strain and two null mutants of the characterized glnB gene (encoding PII) adjacent to glnA. Strains were grown under conditions of nitrogen limitation or nitrogen excess. The proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or...

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Identifiers

PMID: 8763942
DOI: 10.1128/jb.178.14.4143-4149.1996
PMCID: PMC178171

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Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense.PMID 8763942Read ↗

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Mutational analysis of GlnB residues critical for NifA activation in Azospirillum brasilense.Semantic proximity Read ↗

Structural homologues P(II) and P(Z) of Azospirillum brasilense provide intracellular signalling for selective regulation of various nitrogen-dependent functions.Semantic proximity Read ↗

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Cloning and characterisation of the Azospirillum brasilense glnD gene and analysis of a glnD mutant.Semantic proximity Read ↗

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Nitrogenase switch-off by ammonium ions in Azospirillum brasilense requires the GlnB nitrogen signal-transducing protein.Semantic proximity Read ↗

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