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

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Authors:
  • Nielsen, J. ;
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    unknown
  • Kristensen, M. A. ;
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    unknown
  • Willemoes, Martin ;
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    Orcid logo0000-0003-1689-2712
    unknown
  • Nielsen, F. C. ;
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    unknown
  • Christiansen, Jan
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    Orcid logo0000-0001-8624-4601
    unknown
DOI:
10.1093/nar/gkh754
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 ‘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.
Type:
Journal article
Language:
English
Published in:
Nucleic Acids Research, 2004, Vol 32, Issue 14, p. 4368-4376
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2004
Scientific Level:
Scientific
ID:
38778764

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