Transfer-matrix calculations of the effects of tension and torque constraints on DNA-protein interactions

TL;DR

This paper introduces a transfer-matrix theoretical framework to analyze how mechanical forces like tension and torque influence DNA-protein interactions, aiding interpretation of experimental data and understanding DNA organization.

Contribution

The authors developed a systematic transfer-matrix approach to model DNA-protein interactions under mechanical constraints, filling a gap in theoretical tools for this area.

Findings

Predicts effects of force and torque on DNA-binding properties of architectural proteins

Provides insights into mechanical forces' role in chromosomal DNA organization

Enhances interpretation of single-molecule DNA experiments

Abstract

Organization and maintenance of the chromosomal DNA in living cells strongly depends on the DNA interactions with a plethora of DNA-binding proteins. Single-molecule studies show that formation of nucleoprotein complexes on DNA by such proteins is frequently subject to force and torque constraints applied to the DNA. Although the existing experimental techniques allow to exert these type of mechanical constraints on individual DNA biopolymers, their exact effects in regulation of DNA-protein interactions are still not completely understood due to the lack of systematic theoretical methods able to efficiently interpret complex experimental observations. To fill this gap, we have developed a general theoretical framework based on the transfer-matrix calculations that can be used to accurately describe behaviour of DNA-protein interactions under force and torque constraints. Potential applications of the constructed theoretical approach are demonstrated by predicting how these constraints affect the DNA-binding properties of different types of architectural proteins. Obtained results provide important insights into potential physiological functions of mechanical forces in the chromosomal DNA organization by architectural proteins as well as into single-DNA manipulation studies of DNA-protein interactions.