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Nucleic Acids Research 2004 32(14):4368-4376; doi:10.1093/nar/gkh754
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Published online 16 August 2004

Nucleic Acids Research, Vol. 32 No. 14 © Oxford University Press 2004; all rights reserved

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

Jacob Nielsen, Mette Ahm Kristensen, Martin Willemoës1, Finn Cilius Nielsen2 and Jan Christiansen*

Institute of Molecular Biology and 1 Department of Chemistry, University of Copenhagen, Copenhagen, Denmark and 2 Department of Clinical Biochemistry, Rigshospitalet, Copenhagen University Hospital, Copenhagen, Denmark

* To whom correspondence should be addressed at Department of Biological Chemistry, Institute of Molecular Biology, Solvgade 83H, DK-1307 Copenhagen K, Denmark. Tel: +45 3532 2008; Fax: +45 3532 2040; Email: janchr{at}mermaid.molbio.ku.dk

Received May 28, 2004; Revised July 13, 2004; Accepted July 21, 2004

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.


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