The La-related proteins: Structures and interactions of a versatile superfamily of RNA binding proteins

TY - JOUR

T1 - The La-related proteins: Structures and interactions of a versatile superfamily of RNA binding proteins

AU - Conte, Maria Rosaria

PY - 2019/12/3

Y1 - 2019/12/3

N2 - The La-related proteins (LaRPs) are an ancient superfamily of RNA-binding proteins orchestrating the major fates of RNA, from processing and maturation to regulation of mRNA translation. LaRPs are instrumental in modulating complex assemblies where the RNA is bound, folded, processed, escorted and presented to the functional effectors often through recruitment of protein partners. This intricate web of protein-RNA and protein–protein interactions is enabled by the modular nature of the LaRPs, comprising several structured domains connected by flexible linkers, and other sequences lacking recognizable folded motifs. Recent structures, together with biochemical and biophysical studies, have provided insights into how each LaRP family has evolved unique mechanisms of RNA recognition, not only through the conserved RNA-binding unit, the La-module, but also mediated by other family-specific motifs. Furthermore, in a series of unexpected twists and turns, they have revealed that the dynamic and conformational interplay of multi-structured domains and disordered regions operate in unison to achieve RNA substrate discrimination. This review proposes a perspective of our current knowledge of the structure–function relationship of the LaRP superfamily.

AB - The La-related proteins (LaRPs) are an ancient superfamily of RNA-binding proteins orchestrating the major fates of RNA, from processing and maturation to regulation of mRNA translation. LaRPs are instrumental in modulating complex assemblies where the RNA is bound, folded, processed, escorted and presented to the functional effectors often through recruitment of protein partners. This intricate web of protein-RNA and protein–protein interactions is enabled by the modular nature of the LaRPs, comprising several structured domains connected by flexible linkers, and other sequences lacking recognizable folded motifs. Recent structures, together with biochemical and biophysical studies, have provided insights into how each LaRP family has evolved unique mechanisms of RNA recognition, not only through the conserved RNA-binding unit, the La-module, but also mediated by other family-specific motifs. Furthermore, in a series of unexpected twists and turns, they have revealed that the dynamic and conformational interplay of multi-structured domains and disordered regions operate in unison to achieve RNA substrate discrimination. This review proposes a perspective of our current knowledge of the structure–function relationship of the LaRP superfamily.

KW - La-module

KW - La-related proteins

KW - LaRP

KW - RNA biology

KW - RNA-binding proteins

KW - RRM

KW - structure-function relationship

UR - https://www.scopus.com/pages/publications/85075910302

U2 - 10.1080/15476286.2019.1695712

DO - 10.1080/15476286.2019.1695712

M3 - Review article

SN - 1547-6286

JO - Rna Biology

JF - Rna Biology

ER -