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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties. / Dagil, Robert; Ball, Neil J.; Ogrodowicz, Roksana W.; Hobor, Fruzsina; Purkiss, Andrew G.; Kelly, Geoff; Martin, Stephen R.; Taylor, Ian A.; Ramos, Andres.

In: Nucleic Acids Research, Vol. 47, No. 8, 2019, p. 4334-4348.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Dagil, R, Ball, NJ, Ogrodowicz, RW, Hobor, F, Purkiss, AG, Kelly, G, Martin, SR, Taylor, IA & Ramos, A 2019, 'IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties', Nucleic Acids Research, vol. 47, no. 8, pp. 4334-4348. https://doi.org/10.1093/nar/gkz136

APA

Dagil, R., Ball, N. J., Ogrodowicz, R. W., Hobor, F., Purkiss, A. G., Kelly, G., Martin, S. R., Taylor, I. A., & Ramos, A. (2019). IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties. Nucleic Acids Research, 47(8), 4334-4348. https://doi.org/10.1093/nar/gkz136

Vancouver

Dagil R, Ball NJ, Ogrodowicz RW, Hobor F, Purkiss AG, Kelly G et al. IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties. Nucleic Acids Research. 2019;47(8):4334-4348. https://doi.org/10.1093/nar/gkz136

Author

Dagil, Robert ; Ball, Neil J. ; Ogrodowicz, Roksana W. ; Hobor, Fruzsina ; Purkiss, Andrew G. ; Kelly, Geoff ; Martin, Stephen R. ; Taylor, Ian A. ; Ramos, Andres. / IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties. In: Nucleic Acids Research. 2019 ; Vol. 47, No. 8. pp. 4334-4348.

Bibtex

@article{c51cf5f760aa49579b63ae2ea2a15758,
title = "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 RNAbinding 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 pseudodimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.",
author = "Robert Dagil and Ball, {Neil J.} and Ogrodowicz, {Roksana W.} and Fruzsina Hobor and Purkiss, {Andrew G.} and Geoff Kelly and Martin, {Stephen R.} and Taylor, {Ian A.} and Andres Ramos",
year = "2019",
doi = "10.1093/nar/gkz136",
language = "English",
volume = "47",
pages = "4334--4348",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "8",

}

RIS

TY - JOUR

T1 - IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties

AU - Dagil, Robert

AU - Ball, Neil J.

AU - Ogrodowicz, Roksana W.

AU - Hobor, Fruzsina

AU - Purkiss, Andrew G.

AU - Kelly, Geoff

AU - Martin, Stephen R.

AU - Taylor, Ian A.

AU - Ramos, Andres

PY - 2019

Y1 - 2019

N2 - 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 RNAbinding 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 pseudodimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.

AB - 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 RNAbinding 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 pseudodimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.

U2 - 10.1093/nar/gkz136

DO - 10.1093/nar/gkz136

M3 - Journal article

C2 - 30864660

AN - SCOPUS:85068537450

VL - 47

SP - 4334

EP - 4348

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 8

ER -

ID: 229064172