Apr 18, 2020

Disordered Proteins Enable Histone Chaperoning on the Nucleosome

BioRxiv : the Preprint Server for Biology
P. O. HeidarssonBenjamin Schuler

Abstract

Proteins with highly charged disordered regions are abundant in the nucleus, where many of them interact with nucleic acids and control key processes such as transcription. The functional advantages conferred by protein disorder, however, have largely remained unclear. Here we show that disorder can facilitate a remarkable regulatory mechanism involving molecular competition. Single-molecule experiments demonstrate that the human linker histone H1 binds to the nucleosome with ultra-high affinity. However, the large-amplitude dynamics of the positively charged disordered regions of H1 persist on the nucleosome and facilitate the interaction with the highly negatively charged and disordered histone chaperone prothymosin . Consequently, prothymosin can efficiently invade the H1-nucleosome complex and displace H1 via competitive substitution. By integrating experiments and simulations, we establish a molecular model that rationalizes this process structurally and kinetically. Given the abundance of charged disordered regions in the nuclear proteome, this mechanism may be widespread in cellular regulation.

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Mentioned in this Paper

Genome
Genes
Gene Expression
Evaluation
Clone
Genomics
Sequencing
Gene Duplication Abnormality
Polymerase Chain Reaction
Plant Leaves

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