Publication | Closed Access
-Kinked DNA--a Structure That Gives Rise to Drug Intercalation and DNA Breathing--and Its Wider Significance in Determining the Premelting and Melting Behavior of DNA
57
Citations
0
References
1983
Year
DnaDna AnalysisMolecular BiologyGene TranscriptionDrug IntercalationStepwise PolymerizationDna NanotechnologyTranscriptional RegulationNucleic Acid ChemistryProtein FoldingRna Binding ProteinsRna ProcessingBiochemistrySigma FactorOligonucleotideDna ReplicationRna Polymerase EnzymeMelting BehaviorDna BreathingGene ExpressionStructural BiologyBiomolecular EngineeringChromatin FunctionTranscription RegulationChromatinChromatin StructureNatural SciencesNucleic Acid BiochemistryGene RegulationMedicine
One of the major unanswered questions in molecular biology today concerns the ability of a class of proteins known as DNA-binding proteins to recognize specific base sequences in DNA and to bind tightly to these sites. Such noncovalent associations play a key role in regulating gene expression—a process that involves information transfer, first from DNA to RNA and then from RNA to proteins (see Watson 1976; Stryer 1980). The first step in this readout process involves tight binding of a protein known as the RNA polymerase enzyme to specific DNA sites called promoters. The details of this interaction are complex and largely unknown; however, it is generally agreed that at some stage local disruption of hydrogen bonds connecting base pairs occurs to allow the stepwise polymerization of monomelic precursors into RNA. This melting process is assisted by the sigma factor, a protein that binds tightly to the core polymerase enzyme...