Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability
- Authors:
-
- Nielsen, J. ;
- Kristensen, M. A. ;
-
Willemoes, Martin
;
Close
0000-0003-1689-2712
Biomolecular Sciences, Department of Biology, Faculty of Science, Københavns Universitet - Nielsen, F. C. ;
-
Christiansen, Jan
Close0000-0001-8624-4601
Computational and RNA Biology, Department of Biology, Faculty of Science, Københavns Universitet
- 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
