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http://purl.uniprot.org/citations/25691471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25691471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25691471http://www.w3.org/2000/01/rdf-schema#comment"All cells must sense and adapt to changing nutrient availability. However, detailed molecular mechanisms coordinating such regulatory pathways remain poorly understood. In Bacillus subtilis, nitrogen homeostasis is controlled by a unique circuitry composed of the regulator TnrA, which is deactivated by feedback-inhibited glutamine synthetase (GS) during nitrogen excess and stabilized by GlnK upon nitrogen depletion, and the repressor GlnR. Here we describe a complete molecular dissection of this network. TnrA and GlnR, the global nitrogen homeostatic transcription regulators, are revealed as founders of a new structural family of dimeric DNA-binding proteins with C-terminal, flexible, effector-binding sensors that modulate their dimerization. Remarkably, the TnrA sensor domains insert into GS intersubunit catalytic pores, destabilizing the TnrA dimer and causing an unprecedented GS dodecamer-to-tetradecamer conversion, which concomitantly deactivates GS. In contrast, each subunit of the GlnK trimer "templates" active TnrA dimers. Unlike TnrA, GlnR sensors mediate an autoinhibitory dimer-destabilizing interaction alleviated by GS, which acts as a GlnR chaperone. Thus, these studies unveil heretofore unseen mechanisms by which inducible sensor domains drive metabolic reprograming in the model Gram-positive bacterium B. subtilis."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.org/dc/terms/identifier"doi:10.1101/gad.254714.114"xsd:string
http://purl.uniprot.org/citations/25691471http://purl.org/dc/terms/identifier"doi:10.1101/gad.254714.114"xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Schumacher M.A."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Schumacher M.A."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Chinnam N.B."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Chinnam N.B."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Cuthbert B."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Cuthbert B."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Tonthat N.K."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Tonthat N.K."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Whitfill T."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/author"Whitfill T."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/pages"451-464"xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/pages"451-464"xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/title"Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/title"Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis."xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/25691471http://purl.uniprot.org/core/volume"29"xsd:string