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How transcriptional activators bind target proteins.
S Hermann1, K D Berndt, A P Wright
1Department of Natural Sciences, Södertörns högskola, Box 4101, S-14104 Huddinge, Sweden. Stefan.Hermann@sh.se
The Journal of Biological Chemistry
|August 22, 2001
Summary
The proto-oncogene c-Myc
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- The proto-oncogene c-Myc regulates cellular processes by controlling target genes.
- c-Myc protein interacts with transcription factors like TATA-binding protein (TBP) via its transactivation domain (TAD).
Purpose of the Study:
- To investigate the interaction between the c-Myc transactivation domain (TAD) and TATA-binding protein (TBP).
- To elucidate the mechanism and structural requirements for c-Myc TAD binding to TBP.
Main Methods:
- Analysis of c-Myc TAD length requirements for TBP binding.
- Characterization of the kinetic and thermodynamic properties of the c-Myc TAD-TBP interaction.
- Investigation of the nature of interactions (ionic, polar, hydrophobic) during complex formation.
Main Results:
- An extended c-Myc TAD length is necessary for TBP binding, unlike other activators.
- The c-Myc TAD-TBP interaction is a multi-step process.
- Initial complex formation involves ionic/polar interactions, followed by a slow, hydrophobic-driven conversion to a stable complex.
Conclusions:
- The findings reveal specific requirements for c-Myc TAD binding to TBP.
- A two-stage model (rapid low-affinity, slow high-affinity) describes the interaction.
- Proposed models offer a universal paradigm for activator-target factor interactions in gene regulation.