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          Institute: MPI für biophysikalische Chemie     Collection: Molekulare Biologie (Dr. Thomas M. Jovin)     Display Documents



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ID: 169674.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Two functionally redundant isoforms of Drosophila melanogaster eukaryotic initiation factor 4B are involved in cap-dependent translation, cell survival and proliferation
Authors:Hernandez, G.; Vazquez-Pianzola, P.; Zurbriggen, M.; Altmann, M.; Sierra, J. M.; Rivera-Pomar, R.
Language:English
Date of Publication (YYYY-MM-DD):2004-06-23
Title of Journal:European Journal of Biochemistry
Volume:271
Issue / Number:14
Start Page:2923
End Page:2926
Sequence Number of Article:doi:10.1111/j.1432-1033.2004.04217.x
Review Status:not specified
Audience:Not Specified
Abstract / Description:Eukaryotic initiation factor (eIF) 4B is part of the protein complex involved in the recognition and binding of mRNA to the ribosome. Drosophila eIF4B is a single-copy gene that encodes two isoforms, termed eIF4B-L (52.2 kDa) and eIF4B-S (44.2 kDa), generated as a result of the alternative recognition of two polyadeynlation signals during transcription termination and subsequent alternative splicing of the two pre-mRNAs. Both eIF4B mRNAs and proteins are expressed during the entire embryogenesis and life cycle. The proteins are cytoplasmic with polarized distribution. The two isoforms bindRNAwith the same affinity. eIF4B-L and eIF4B-S preferentially enhance cap-dependent over IRES-dependent translation initiation in a Drosophila cellfree translation system. RNA interference experiments suggest that eIF4B is required for cell survival, although only a modest reduction in rate of protein synthesis is observed. Overexpression of eIF4B in Drosophila cells in culture and in developing eye imaginal discs promotes cell proliferation.
Free Keywords:cell survival; Drosophila; eukaryotic initiation factor 4B (eIF4B); proliferation; translation
Last Change of the Resource (YYYY-MM-DD):2004-07-05
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
External Affiliations:Institut für Biochemie und Molekularbiologie, Universität Bern, Switzerland; Centro de Biología Molecular 'Severo Ochoa', Universidad Autónoma de Madrid, Spain
Identifiers:URL:http://www3.interscience.wiley.com/cgi-bin/fulltex...
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