title: The N-terminal domain of Aliivibrio fischeri LuxR is a target of the GroEL chaperonin.
abstract: Here we show that the C-terminal domain of LuxR activates the transcription of Aliivibrio fischeri luxICDABEG in Escherichia coli SKB178 gro(+) and E. coli OFB1111 groEL673 strains to the same level. Using affinity chromatography, we showed that GroEL binds to the N-terminal domain of LuxR, pointing to a GroEL/GroES requirement for the folding of the N-terminal domain of LuxR.
authors: State Research Institute of Genetics and Selection of Industrial Microorganisms Genetika, 1st Dorozhnii pr 1, 117545 Moscow, Russia. manukhov@genetika.ru
authors: Ilya V
authors: IV
authors: Manukhov
authors: Ol'ga E
authors: OE
authors: Melkina
authors: Ignatii I
authors: II
authors: Goryanin
authors: Ancha V
authors: AV
authors: Baranova
authors: Gennadii B
authors: GB
authors: Zavilgelsky
mesh_terms: D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D009154:Mutation; D017434:Protein Structure, Tertiary; D053038:Quorum Sensing; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D013312:Stress, Physiological; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism*; D014737:Vibrionaceae / Q000235:genetics* / Q000378:metabolism*
chemical_list: D018834:Chaperonin 60; D012097:Repressor Proteins; D015534:Trans-Activators; C064778:LuxR autoinducer binding proteins