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IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties.

Abstract：

:IGF2 mRNA-binding protein 1 (IMP1) is a key regulator of messenger RNA (mRNA) metabolism and transport in organismal development and, in cancer, its mis-regulation is an important component of tumour metastasis. IMP1 function relies on the recognition of a diverse set of mRNA targets that is mediated by the combinatorial action of multiple RNA-binding domains. Here, we dissect the structure and RNA-binding properties of two key RNA-binding domains of IMP1, KH1 and KH2, and we build a kinetic model for the recognition of RNA targets. Our data and model explain how the two domains are organized as an intermolecular pseudo-dimer and that the important role they play in mRNA target recognition is underpinned by the high RNA-binding affinity and fast kinetics of this KH1KH2-RNA recognition unit. Importantly, the high-affinity RNA-binding by KH1KH2 is achieved by an inter-domain coupling 50-fold stronger than that existing in a second pseudo-dimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Dagil R,Ball NJ,Ogrodowicz RW,Hobor F,Purkiss AG,Kelly G,Martin SR,Taylor IA,Ramos A

doi

10.1093/nar/gkz136

subject

Has Abstract

pub_date

2019-05-07 00:00:00

pages

4334-4348

issue

8

eissn

0305-1048

issn

1362-4962

pii

5377473

journal_volume

47

pub_type

杂志文章

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