Search by proteins for their DNA target site: 1. The effect of DNA conformation on protein sliding.

ABSTRACT: The recognition of DNA-binding proteins (DBPs) to their specific site often precedes by a search technique in which proteins slide, hop along the DNA contour or perform inter-segment transfer and 3D diffusion to dissociate and re-associate to distant DNA sites. In this study, we demonstrated that the strength and nature of the non-specific electrostatic interactions, which govern the search dynamics of DBPs, are strongly correlated with the conformation of the DNA. We tuned two structural parameters, namely curvature and the extent of helical twisting in circular DNA. These two factors are mutually independent of each other and can modulate the electrostatic potential through changing the geometry of the circular DNA conformation. The search dynamics for DBPs on circular DNA is therefore m

SUBMITTER: Bhattacherjee A 

PROVIDER: S-EPMC4227778 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature