Linker regions of the RhaS and RhaR proteins.
Substitutions within the interdomain linkers of the AraC/XylS family proteins RhaS and RhaR were tested to determine whether side chain identity or linker structure was required for function. Neither was found crucial, suggesting that the linkers do not play a direct role in activation, but rather simply connect the two domains.
Kolin
Ana
A
Department of Molecular Biosciences, 1200 Sunnyside Ave., University of Kansas, Lawrence, KS 66045, USA.
Jevtic
Visnja
V
Swint-Kruse
Liskin
L
Egan
Susan M
SM
D000409:Alanine / Q000235:genetics; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D051777:AraC Transcription Factor / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012210:Rhamnose / Q000378:metabolism; D016415:Sequence Alignment; D015534:Trans-Activators / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000502:physiology*
D051777:AraC Transcription Factor; C497371:AraC protein, E coli; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C062863:RhaR protein, E coli; C084095:RhaS protein, E coli; D015534:Trans-Activators; D014157:Transcription Factors; D000409:Alanine; D012210:Rhamnose