Thermodynamic modeling reveals widespread multivalent binding by RNA-binding proteins.

ABSTRACT:

Motivation

Understanding how proteins recognize their RNA targets is essential to elucidate regulatory processes in the cell. Many RNA-binding proteins (RBPs) form complexes or have multiple domains that allow them to bind to RNA in a multivalent, cooperative manner. They can thereby achieve higher specificity and affinity than proteins with a single RNA-binding domain. However, current approaches to de novo discovery of RNA binding motifs do not take multivalent binding into account.

Results

We present Bipartite Motif Finder (BMF), which is based on a thermodynamic model of RBPs with two cooperatively binding RNA-binding domains. We show that bivalent binding is a common strategy among RBPs, yielding higher affinity and sequence specificity. We furthermore illustrate that t

SUBMITTER: Sohrabi-Jahromi S 

PROVIDER: S-EPMC8275352 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature