Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability

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

Standard

Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. / Nielsen, J.; Kristensen, M. A.; Willemoes, Martin; Nielsen, F. C.; Christiansen, Jan.

In: Nucleic Acids Research, Vol. 32, No. 14, 2004, p. 4368-4376.

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

Harvard

Nielsen, J, Kristensen, MA, Willemoes, M, Nielsen, FC & Christiansen, J 2004, 'Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability', Nucleic Acids Research, vol. 32, no. 14, pp. 4368-4376. https://doi.org/10.1093/nar/gkh754

APA

Nielsen, J., Kristensen, M. A., Willemoes, M., Nielsen, F. C., & Christiansen, J. (2004). Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. Nucleic Acids Research, 32(14), 4368-4376. https://doi.org/10.1093/nar/gkh754

Vancouver

Nielsen J, Kristensen MA, Willemoes M, Nielsen FC, Christiansen J. Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. Nucleic Acids Research. 2004;32(14):4368-4376. https://doi.org/10.1093/nar/gkh754

Author

Nielsen, J. ; Kristensen, M. A. ; Willemoes, Martin ; Nielsen, F. C. ; Christiansen, Jan. / Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. In: Nucleic Acids Research. 2004 ; Vol. 32, No. 14. pp. 4368-4376.

Bibtex

@article{a3d176e074c311dbbee902004c4f4f50,
title = "Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability",
abstract = "Active cytoplasmic RNA localization depends on the attachment of RNA-binding proteins that dictate the destination of the RNA molecule. In this study, we used an electrophoretic mobility-shift assay in combination with equilibrium and kinetic analyses to characterize the assembly of the human zipcode-binding protein IMP1 on targets in the 3'-UTR from Igf-II mRNA and in H19 RNA. In both cases, two molecules of IMP1 bound to RNA by a sequential, cooperative mechanism, characterized by an initial fast step, followed by a slow second step. The first step created an obligatory assembly intermediate of low stability, whereas the second step was the discriminatory event that converted a putative RNA target into a {\textquoteleft}locked' stable RNP. The ability to dimerize was also observed between members of the IMP family of zipcode-binding proteins, providing a multitude of further interaction possibilities within RNP granules and with the localization apparatus. ",
author = "J. Nielsen and Kristensen, {M. A.} and Martin Willemoes and Nielsen, {F. C.} and Jan Christiansen",
year = "2004",
doi = "10.1093/nar/gkh754",
language = "English",
volume = "32",
pages = "4368--4376",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "14",

}

RIS

TY - JOUR

T1 - Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability

AU - Nielsen, J.

AU - Kristensen, M. A.

AU - Willemoes, Martin

AU - Nielsen, F. C.

AU - Christiansen, Jan

PY - 2004

Y1 - 2004

N2 - Active cytoplasmic RNA localization depends on the attachment of RNA-binding proteins that dictate the destination of the RNA molecule. In this study, we used an electrophoretic mobility-shift assay in combination with equilibrium and kinetic analyses to characterize the assembly of the human zipcode-binding protein IMP1 on targets in the 3'-UTR from Igf-II mRNA and in H19 RNA. In both cases, two molecules of IMP1 bound to RNA by a sequential, cooperative mechanism, characterized by an initial fast step, followed by a slow second step. The first step created an obligatory assembly intermediate of low stability, whereas the second step was the discriminatory event that converted a putative RNA target into a ‘locked' stable RNP. The ability to dimerize was also observed between members of the IMP family of zipcode-binding proteins, providing a multitude of further interaction possibilities within RNP granules and with the localization apparatus.

AB - Active cytoplasmic RNA localization depends on the attachment of RNA-binding proteins that dictate the destination of the RNA molecule. In this study, we used an electrophoretic mobility-shift assay in combination with equilibrium and kinetic analyses to characterize the assembly of the human zipcode-binding protein IMP1 on targets in the 3'-UTR from Igf-II mRNA and in H19 RNA. In both cases, two molecules of IMP1 bound to RNA by a sequential, cooperative mechanism, characterized by an initial fast step, followed by a slow second step. The first step created an obligatory assembly intermediate of low stability, whereas the second step was the discriminatory event that converted a putative RNA target into a ‘locked' stable RNP. The ability to dimerize was also observed between members of the IMP family of zipcode-binding proteins, providing a multitude of further interaction possibilities within RNP granules and with the localization apparatus.

U2 - 10.1093/nar/gkh754

DO - 10.1093/nar/gkh754

M3 - Journal article

C2 - 15314207

VL - 32

SP - 4368

EP - 4376

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 14

ER -

ID: 98354