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Light‐Regulated Tetracycline Binding to the Tet Repressor
Author(s) -
Moon Jayoung,
Gam Jongsik,
Lee SeungGoo,
Suh YoungGer,
Lee Jeeyeon
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201304027
Subject(s) - tetr , repressor , chemistry , photoswitch , biophysics , allosteric regulation , ligand (biochemistry) , computational biology , biology , biochemistry , transcription factor , receptor , photochemistry , gene
Elucidation of the signal‐transmission pathways between distant sites within proteins is of great importance in medical and bioengineering sciences. The use of optical methods to redesign protein functions is emerging as a general approach for the control of biological systems with high spatiotemporal precision. Here we report the detailed thermodynamic and kinetic characterization of novel chimeric light‐regulated Tet repressor (TetR) switches in which light modulates the TetR function. Light absorbed by flavin mononucleotide (FMN) generates a signal that is transmitted to As‐LOV and YtvA‐LOV fused TetR proteins (LOV=light–oxygen–voltage), in which it alters the binding to tetracycline, the TetR ligand. The engineering of light‐sensing protein modules with TetR is a valuable tool that deepens our understanding of the mechanism of signal transmission within proteins. In addition, the light‐regulated changes of drug binding that we describe here suggest that engineered light‐sensitive proteins may be used for the development of novel therapeutic strategies.