MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nielsen, J.
Right arrow Articles by Nielsen, F. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nielsen, J.
Right arrow Articles by Nielsen, F. C.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 1999, p. 1262-1270, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Family of Insulin-Like Growth Factor II mRNA-Binding Proteins Represses Translation in Late Development

Jacob Nielsen,1 Jan Christiansen,1,* Jens Lykke-Andersen,1 Anders H. Johnsen,3 Ulla M. Wewer,2 and Finn C. Nielsen3

RNA Regulation Centre, Institute of Molecular Biology,1 and Institute of Molecular Pathology,2 University of Copenhagen, and Department of Clinical Biochemistry, Rigshospitalet,3 Copenhagen, Denmark

Received 28 September 1998/Returned for modification 27 October 1998/Accepted 9 November 1998

Insulin-like growth factor II (IGF-II) is a major fetal growth factor. The IGF-II gene generates multiple mRNAs with different 5' untranslated regions (5' UTRs) that are translated in a differential manner during development. We have identified a human family of three IGF-II mRNA-binding proteins (IMPs) that exhibit multiple attachments to the 5' UTR from the translationally regulated IGF-II leader 3 mRNA but are unable to bind to the 5' UTR from the constitutively translated IGF-II leader 4 mRNA. IMPs contain the unique combination of two RNA recognition motifs and four hnRNP K homology domains and are homologous to the Xenopus Vera and chicken zipcode-binding proteins. IMP localizes to subcytoplasmic domains in a growth-dependent and cell-specific manner and causes a dose-dependent translational repression of IGF-II leader 3 -luciferase mRNA. Mouse IMPs are produced in a burst at embryonic day 12.5 followed by a decline towards birth, and, similar to IGF-II, IMPs are especially expressed in developing epithelia, muscle, and placenta in both mouse and human embryos. The results imply that cytoplasmic 5' UTR-binding proteins control IGF-II biosynthesis during late mammalian development.

* Corresponding author. Mailing address: Institute of Molecular Biology, University of Copenhagen, Sølvgade 83 H, DK-1307 Copenhagen K, Denmark. Phone: 45 35 32 20 08. Fax: 45 35 32 20 40. E-mail: janchr{at}mermaid.molbio.ku.dk.

Molecular and Cellular Biology, February 1999, p. 1262-1270, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 1999 by the American Society for Microbiology. All rights reserved.