Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions

Schütz, Patrick; Bumann, Mario; Oberholzer, Anselm Erich; Bieniossek, Christoph; Trachsel, Hans; Altmann, Michael; Baumann, Ulrich (2008). Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 105(28), pp. 9564-9569. Washington, D.C.: National Academy of Sciences NAS 10.1073/pnas.0800418105

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Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-A resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Schütz, Patrick; Oberholzer, Anselm; Trachsel, Hans; Altmann, Michael and Baumann, Ulrich

ISSN:

0027-8424

Publisher:

National Academy of Sciences NAS

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 15:05

Last Modified:

06 Dec 2013 13:54

Publisher DOI:

10.1073/pnas.0800418105

PubMed ID:

18606994

Web of Science ID:

000257784700022

URI:

https://boris.unibe.ch/id/eprint/28312 (FactScience: 119818)

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