On the specificity of DNA-protein interactions.
AUTOR(ES)
von Hippel, P H
RESUMO
In this paper we summarize the various factors that must be considered in establishing the operational specificity of the binding of a protein regulator of gene expression to a DNA target site. We consider informational (combinatorial) aspects of binding-site specification, actual recognition mechanisms, and the thermodynamics of target-site selection against a background of competing pseudospecific and non-(sequence)-specific DNA binding sites. The results provide insight into the design, specification, and possibly the evolution of regulatory proteins and their chromosomal binding targets, as well as into practical aspects of the design of regulatory-protein isolation schemes and physicochemical regulatory considerations in vivo.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=323132Documentos Relacionados
- Thymine methyls and DNA-protein interactions.
- Missing contact probing of DNA-protein interactions.
- Polyamines alter sequence-specific DNA-protein interactions.
- Kinetics of RNA polymerase-promoter complex formation: effects of nonspecific DNA-protein interactions.
- Review: ethidium fluorescence assay. Part II. Enzymatic studies and DNA-protein interactions.