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Allosteric regulation within the highly interconnected structural scaffold of AraC/XylS homologs tolerates a wide range of amino acid changes.
Picard HR, Schwingen KS, Green LM, Shis DL, Egan SM, Bennett MR, Swint-Kruse L
Proteins. 2021 Aug 8. doi: 10.1002/prot.26206.
PubMed Article

Plasmids from Article

ID Plasmid Purpose
170107UUUUA-pHG165cConstitutively expressed, chimeric transcription activator comprising the AraC DNA binding domain and the UreR urea ligand binding domain.
170108MMMMA-pHG165cConstitutively expressed, chimeric transcription activator comprising the AraC DNA binding domain and the MelR L-melibiose ligand binding domain.
170110XXXXA-pHG165cConstitutively expressed, chimeric transcription activator comprising the AraC DNA binding domain and the XylS benzoate ligand binding domain.
170111XXXXA_Q182A_R287H-pHG165cConstitutively expressed , mutationally-enhanced chimeric transcription activator comprising the AraC DNA binding domain and the XylS benzoate ligand binding domain.
170112RRRAA-pHG165cConstitutively expressed, chimeric transcription activator comprising the AraC DNA binding domain and the RhaR rhamnose ligand binding domains.
170113RRRAA-5-mut-pHG165cConstitutively expressed, mutationally-enhanced chimeric transcription activator comprising the AraC DNA binding domain and the RhaR rhamnose ligand binding domains.
170114AraC-pHG165c WTConstitutively expressed, wild-type E coli AraC transcription activator; activated by L-Arabinose.
172602BW-ParaThe BW-Para E. coli strain is used to screen the functions of chimeric AraC/XylS transcription activators using beta-galactosidase assays.

Antibodies from Article