How RNA-Binding Proteins Interact with RNA: Molecules and Mechanisms

RNA-binding proteins (RBPs) comprise a large class of over 2,000 proteins that interact with transcripts in all manner of RNA-driven processes. The structures and mechanisms that RBPs use to bind and regulate RNA are incredibly diverse. In this review, we take a look at the components of protein-RNA...

Full description

Saved in:
Bibliographic Details
Published in:Molecular cell Vol. 78; no. 1; p. 9
Main Authors: Corley, Meredith, Burns, Margaret C, Yeo, Gene W
Format: Journal Article
Language:English
Published: United States 02.04.2020
Subjects:
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Protein Binding
RNA - chemistry
RNA - metabolism
RNA-Binding Motifs
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
Software
(∗)Insert Keywords Here(∗)
ISSN:1097-4164, 1097-4164
Online Access:Get more information
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:RNA-binding proteins (RBPs) comprise a large class of over 2,000 proteins that interact with transcripts in all manner of RNA-driven processes. The structures and mechanisms that RBPs use to bind and regulate RNA are incredibly diverse. In this review, we take a look at the components of protein-RNA interaction, from the molecular level to multi-component interaction. We first summarize what is known about protein-RNA molecular interactions based on analyses of solved structures. We additionally describe software currently available for predicting protein-RNA interaction and other resources useful for the study of RBPs. We then review the structure and function of seventeen known RNA-binding domains and analyze the hydrogen bonds adopted by protein-RNA structures on a domain-by-domain basis. We conclude with a summary of the higher-level mechanisms that regulate protein-RNA interactions.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:1097-4164
1097-4164
DOI:10.1016/j.molcel.2020.03.011