The study of the plant oncogene rolA has been hampered by a lack of structural information. Here we show that, despite a lack of significant sequence similarity to proteins of known structure, the rolA sequence adopts a known fold; that of the papillomavirus E2 DNA-binding domain. This fold is relia
A Model for Protein–DNA Interaction Dynamics
✍ Scribed by P. ETCHEGOIN; M. NÖLLMANN
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 240 KB
- Volume
- 220
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
✦ Synopsis
We map a simplified version of the protein-DNA interaction problem into an Ising-model in a random magnetic field. The model includes a "head" which moves along the chain while interacting with the underlying spins. The head moves by using the statistical fluctuations of base openings. A Monte Carlo (MC) simulation of this model reveals the possibility of biased diffusion in one direction, followed by sequence identification and binding. The model provides some insight into the mechanisms used by some repressor proteins to diffuse and bind to specific DNA-binding sites.
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