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Protein-DNA interfaces: a molecular dynamics analysis of time-dependent recognition processes for three transcription factors.

ABSTRACT: We have studied the dynamics of three transcription factor-DNA complexes using all-atom, microsecond-scale MD simulations. In each case, the salt bridges and hydrogen bond interactions formed at the protein-DNA interface are found to be dynamic, with lifetimes typically in the range of tens to hundreds of picoseconds, although some interactions, notably those involving specific binding to DNA bases, can be a hundred times longer lived. Depending on the complex studied, this dynamics may or may not lead to the existence of distinct conformational substates. Using a sequence threading technique, it has been possible to determine whether DNA sequence recognition is sensitive or not to such conformational changes, and, in one case, to show that recognition appears to be locally dependent on protein-mediated cation distributions.

SUBMITTER: Etheve L

PROVIDER: S-EPMC5175364 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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Protein-DNA interfaces: a molecular dynamics analysis of time-dependent recognition processes for three transcription factors.

Etheve Loïc L Martin Juliette J Lavery Richard R

Nucleic acids research 20160921 20

We have studied the dynamics of three transcription factor-DNA complexes using all-atom, microsecond-scale MD simulations. In each case, the salt bridges and hydrogen bond interactions formed at the protein-DNA interface are found to be dynamic, with lifetimes typically in the range of tens to hundreds of picoseconds, although some interactions, notably those involving specific binding to DNA bases, can be a hundred times longer lived. Depending on the complex studied, this dynamics may or may n ...[more]

PMID: 27658967

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