Interaction between GlnB and the N-terminal domain of NifA in Azospirillum brasilense

Zhou, Xiaoyu; Zou, Xuefeng; Li, Jilun

doi:10.1007/s11434-008-0435-x

Cited by 3 publications

(4 citation statements)

References 21 publications

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“…Previous results have shown that the NifA protein from A. brasilense requires co-expression of the cognate GlnB protein to activate nif gene expression in an E. coli background ( 8 ). In its native background, the NifA activity is regulated by the prevailing ammonium levels and the N-terminal GAF domain of NifA has been implicated in ammonium-dependent regulation through interaction with the GlnB protein ( 5 , 7 ).…”

Section: Resultsmentioning

confidence: 99%

“…It has been proposed that this control involves direct interaction between the NifA GAF domain and the GlnB protein in A. brasilense ( 6 , 7 ). This model suggests that GlnB binds to NifA under low levels of fixed nitrogen and relieves the inhibition by the GAF domain of the central AAA+ domain ( 5 - 8 ). Recent studies have shown that amino acid residues 66-88 and 165-176 in the NifA GAF domain are responsible for the interaction with GlnB ( 8 ).…”

Section: Introductionmentioning

confidence: 99%

“…This model suggests that GlnB binds to NifA under low levels of fixed nitrogen and relieves the inhibition by the GAF domain of the central AAA+ domain ( 5 - 8 ). Recent studies have shown that amino acid residues 66-88 and 165-176 in the NifA GAF domain are responsible for the interaction with GlnB ( 8 ). GlnB is a homotrimeric protein of the P II family that can sense the cellular nitrogen, carbon and energy levels and relay these signals to a variety of target proteins by means of protein-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

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Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense

Sotomaior

Araújo

Nishikawa

et al. 2012

Braz J Med Biol Res

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Azospirillum brasilense is a diazotroph that associates with important agricultural crops and thus has potential to be a nitrogen biofertilizer. The A. brasilense transcription regulator NifA, which seems to be constitutively expressed, activates the transcription of nitrogen fixation genes. It has been suggested that the nitrogen status-signaling protein GlnB regulates NifA activity by direct interaction with the NifA N-terminal GAF domain, preventing the inhibitory effect of this domain under conditions of nitrogen fixation. In the present study, we show that an N-terminal truncated form of NifA no longer required GlnB for activity and lost regulation by ammonium. On the other hand, in trans co-expression of the N-terminal GAF domain inhibited the N-truncated protein in response to fixed nitrogen levels. We also used pull-down assays to show in vitro interaction between the purified N-terminal GAF domain of NifA and the GlnB protein. The results showed that A. brasilense GlnB interacts directly with the NifA N-terminal domain and this interaction is dependent on the presence of ATP and 2-oxoglutarate.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense

Sotomaior

Araújo

Nishikawa

et al. 2012

Braz J Med Biol Res

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“…However, NtrC is not involved in the expression of nifA in A. brasilense, but is involved in K. pneuomoniae. It is proposed that oxygen may be involved directly in the post-translational regulation of NifA activity, since NifA contains a motif of cysteine residues (Araujo et al 2004;Zhou et al 2008). So far, the mechanism of regulation of nifA expression in A. brasilense is not well known.…”

Section: Introductionmentioning

confidence: 99%

Functional analysis of the fixL/fixJ and fixK genes in Azospirillum brasilense Sp7

Ren

et al. 2010

Ann Microbiol

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This study demonstrates for the first time that the two-component FixL/FixJ system, activating expression of nitrogen fixation genes in response to low oxygen concentration in rhizobia, also exists in Azospirillum brasilense Sp7. A heme staining assay showed that A. brasilense FixL contains a heme cofactor like that of rhizobial FixL proteins. Azospirillum brasilense FixL and FixJ could activate expression of Sinorhizobium meliloti nifA in S. meliloti fixL − and fixJ − mutants and in Escherichia coli, and that activation was dependent on oxygen concentration, indicating that A. brasilense FixL and FixJ have the same function as S. meliloti FixL and FixJ. Azospirillum brasilense FixL and FixJ could activate expression of A. brasilense fixK in E. coli. Azospirillum brasilense FixL, FixJ, and FixK positively regulated expression of A. brasilense nifA in A. brasilense strains but not in E. coli. The results show that FixL and FixJ can activate the fixK expression, with FixK subsequently activating nifA expression in A. brasilense. Azospirillum brasilense fixJ was involved in aerotaxis and S. meliloti fixJ could restore aerotaxis of the A. brasilense fixJ − mutant. Mutations in fixL and fixJ did not affect nitrogen fixation.

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Genetically engineered deletion in the N-terminal region of nifA1 in R. capsulatus to enhance hydrogen production

Gao

Xuan

Wang

et al. 2023

International Journal of Hydrogen Energy

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Interaction between GlnB and the N-terminal domain of NifA in Azospirillum brasilense

Cited by 3 publications

References 21 publications

Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense

Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense

Functional analysis of the fixL/fixJ and fixK genes in Azospirillum brasilense Sp7

Genetically engineered deletion in the N-terminal region of nifA1 in R. capsulatus to enhance hydrogen production

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