Structural Mechanism behind Distinct Efficiency of Oct4/Sox2 Proteins in Differentially Spaced DNA Complexes.

ABSTRACT: The octamer-binding transcription factor 4 (Oct4) and sex-determining region Y (SRY)-box 2 (Sox2) proteins induce various transcriptional regulators to maintain cellular pluripotency. Most Oct4/Sox2 complexes have either 0 base pairs (Oct4/Sox2(0bp)) or 3 base pairs (Oct4/Sox2(3bp)) separation between their DNA-binding sites. Results from previous biochemical studies have shown that the complexes separated by 0 base pairs are associated with a higher pluripotency rate than those separated by 3 base pairs. Here, we performed molecular dynamics (MD) simulations and calculations to determine the binding free energy and per-residue free energy for the Oct4/Sox2(0bp) and Oct4/Sox2(3bp) complexes to identify structural differences that contribute to differences in induction rate. Our MD simulati

SUBMITTER: Yesudhas D 

PROVIDER: S-EPMC4720428 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature