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Molecular and Cellular Biology, October 2005, p. 9028-9039, Vol. 25, No. 20
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.20.9028-9039.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Xenopus ELAV Protein ElrB Represses Vg1 mRNA Translation during Oogenesis

Lucy J. Colegrove-Otero,{dagger} Agathe Devaux,{dagger} and Nancy Standart*

Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom

Received 12 November 2004/ Returned for modification 13 December 2004/ Accepted 29 June 2005

Xenopus laevis Vg1 mRNA undergoes both localization and translational control during oogenesis. We previously characterized a 250-nucleotide AU-rich element, the Vg1 translation element (VTE), in the 3'-untranslated region (UTR) of this mRNA that is responsible for the translational repression. UV-cross-linking and immunoprecipitation experiments, described here, revealed that the known AU-rich element binding proteins, ElrA and ElrB, and TIA-1 and TIAR interact with the VTE. The levels of these proteins during oogenesis are most consistent with a possible role for ElrB in the translational control of Vg1 mRNA, and ElrB, in contrast to TIA-1 and TIAR, is present in large RNP complexes. Immunodepletion of TIA-1 and TIAR from Xenopus translation extract confirmed that these proteins are not involved in the translational repression. Mutagenesis of a potential ElrB binding site destroyed the ability of the VTE to bind ElrB and also abolished translational repression. Moreover, multiple copies of the consensus motif both bind ElrB and support translational control. Therefore, there is a direct correlation between ElrB binding and translational repression by the Vg1 3'-UTR. In agreement with the reporter data, injection of a monoclonal antibody against ElrB into Xenopus oocytes resulted in the production of Vg1 protein, arguing for a role for the ELAV proteins in the translational repression of Vg1 mRNA during early oogenesis.


* Corresponding author. Mailing address: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom. Phone: 01223 333673. Fax: 01223 766002. E-mail: nms{at}mole.bio.cam.ac.uk.

{dagger} Authors contributed equally.


Molecular and Cellular Biology, October 2005, p. 9028-9039, Vol. 25, No. 20
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.20.9028-9039.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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