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Superrepression through Altered Corepressor–Activated Protein:Protein Interactions
- Source :
- Biochemistry. 57:1119-1129
- Publication Year :
- 2018
- Publisher :
- American Chemical Society (ACS), 2018.
-
Abstract
- Small molecules regulate transcription in both eukaryotes and prokaryotes by either enhancing or repressing assembly of transcription regulatory complexes. For allosteric transcription repressors, superrepressor mutants can exhibit increased sensitivity to small molecule corepressors. However, because many transcription regulatory complexes assemble in multiple steps, the superrepressor phenotype can reflect changes in any or all of the individual assembly steps. Escherichia coli biotin operon repression complex assembly, which responds to input biotin concentration, occurs via three coupled equilibria, including corepressor binding, holorepressor dimerization, and binding of the dimer to DNA. A genetic screen has yielded superrepressor mutants that repress biotin operon transcription in vivo at biotin concentrations much lower than those required by the wild type repressor. In this work, isothermal titration calorimetry and sedimentation measurements were used to determine the superrepressor biotin binding and homodimerization properties. The results indicate that, although all variants exhibit biotin binding affinities similar to that measured for BirA
- Subjects :
- 0301 basic medicine
Biotin binding
Protein Conformation
Operon
Biotin
Repressor
Molecular Dynamics Simulation
Biochemistry
Protein–protein interaction
03 medical and health sciences
chemistry.chemical_compound
Allosteric Regulation
Transcription (biology)
Escherichia coli
Carbon-Nitrogen Ligases
Protein Interaction Maps
030102 biochemistry & molecular biology
Escherichia coli Proteins
Isothermal titration calorimetry
Cell biology
Repressor Proteins
030104 developmental biology
chemistry
Thermodynamics
Protein Multimerization
Corepressor
Protein Binding
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 57
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....1279188c2cee95dee3bd5e8af5cee385