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...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:Molecular cell Ročník 78; číslo 1; s. 9
Hlavní autori: Corley, Meredith, Burns, Margaret C, Yeo, Gene W
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 02.04.2020
Predmet:
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
On-line prístup:Zistit podrobnosti o prístupe
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí: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.
Bibliografia: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