How do DNA-bound proteins leave their binding sites? The role of facilitated dissociation

Aykut Erbaş, John F. Marko

Research output: Contribution to journalReview article

1 Scopus citations

Abstract

Dissociation of a protein from DNA is often assumed to be described by an off rate that is independent of other molecules in solution. Recent experiments and computational analyses have challenged this view by showing that unbinding rates (residence times) of DNA-bound proteins can depend on concentrations of nearby molecules that are competing for binding. This ‘facilitated dissociation’ (FD) process can occur at the single-binding site level via formation of a ternary complex, and can dominate over ‘spontaneous dissociation’ at low (submicromolar) concentrations. In the crowded intracellular environment FD introduces new regulatory possibilities at the level of individual biomolecule interactions.

Original languageEnglish (US)
Pages (from-to)118-124
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume53
DOIs
StatePublished - Dec 2019

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

Fingerprint Dive into the research topics of 'How do DNA-bound proteins leave their binding sites? The role of facilitated dissociation'. Together they form a unique fingerprint.

  • Cite this