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2020
DOI: 10.1016/j.bbapap.2019.140348
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Regulation of Herbaspirillum seropedicae NifA by the GlnK PII signal transduction protein is mediated by effectors binding to allosteric sites

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Cited by 7 publications
(3 citation statements)
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“…It had been assumed for quite a while that the Mg 2+ -ATP + 2-OGcomplexed state and post-translational modification of PII prevents any interaction of PII with other targets. Recently, however, PII targets have been identified which select these states [41][42][43]. This highlights the sensing and structural flexibility in PII signaling (see e.g., [21,[26][27][28])…”
Section: Open Accessmentioning
confidence: 99%
“…It had been assumed for quite a while that the Mg 2+ -ATP + 2-OGcomplexed state and post-translational modification of PII prevents any interaction of PII with other targets. Recently, however, PII targets have been identified which select these states [41][42][43]. This highlights the sensing and structural flexibility in PII signaling (see e.g., [21,[26][27][28])…”
Section: Open Accessmentioning
confidence: 99%
“…The N–terminal PAS domain can bind and hydrolyze ATP, but only the C–terminal domain can form the stabilized complex with NifA [ 63 ]. Besides γ–proteobacteria, NifL homologs have also been characterized in α–, β–, and ζ–proteobacteria, but few studies have described the regulation of NifL in these proteobacteria [ 64 , 65 ].…”
Section: The Differences In the Nifa–nifl System For The Different Ni...mentioning
confidence: 99%
“…Ammonium ions through a mechanism involving its N-terminal domain control the activity of NifA, and Nterminal domain inhibits NifA-dependent transcriptional activation by an inter-domain cross-talk between the catalytic domain of the NifA protein and its regulatory N-terminal domain in response to fixed nitrogen (Monteiro et al, 2001). The activity of NifA is negatively influenced by oxygen (Monteiro et al, 1999;Souza et al, 1999;Oliveira et al, 2009), but interaction with Glnk positively influence it, and binding of 2-OG and MgATP to Glnk are very important for NifA activation (Stefanello et al, 2020). Its oxygen sensitivity may attribute to a conserved motif of cysteine residues in NifA which spans the central AAA+ domain and the interdomain linker which connects the AAA+ domain to the C-terminal DNA binding domain (Oliveira et al, 2009).…”
Section: Bradyrhizobium Bradyrhizobium Bradyrhizobium Bradyrhizobiummentioning
confidence: 99%