The N-terminal domain of Aliivibrio fischeri LuxR is a target of the GroEL chaperonin.
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.
Manukhov
Ilya V
IV
State Research Institute of Genetics and Selection of Industrial Microorganisms Genetika, 1st Dorozhnii pr 1, 117545 Moscow, Russia. manukhov@genetika.ru
Melkina
Ol'ga E
OE
Goryanin
Ignatii I
II
Baranova
Ancha V
AV
Zavilgelsky
Gennadii B
GB
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*
D018834:Chaperonin 60; D012097:Repressor Proteins; D015534:Trans-Activators; C064778:LuxR autoinducer binding proteins