Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation  . Issue 3 (18th May 2017)

• Record Type: Journal Article
• Authors: Miras, Manuel; Truniger, Verónica; Silva, Cristina; Verdaguer, Núria; Aranda, Miguel A.; Querol-Audí, Jordi
• Is Part Of: Plant physiology. Volume 174:Issue 3(2017)
• Page Start: 1476
• Page End: 1491
• Publication Date: 2017-05-18
• Subjects: Plant physiology -- Periodicals; Botany -- Periodicals; Periodicals; Electronic journals; 571.2
• DOI: 10.1104/pp.17.00193
• Languages: English
• ISSNs: 0032-0889

Abstract

Abstract : The first structure of a plant eIF4E bound to an eIF4G interacting peptide supports a universal mechanism of regulation of translation initiation in higher eukaryotes. Abstract: The association-dissociation of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation. The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a single canonical alpha-helical motif, while metazoan eIF4E-binding proteins (m4E-BPs) advantageously compete against eIF4G via bimodal interactions involving this canonical motif and a second noncanonical motif of the eIF4E surface. Metazoan eIF4Gs share this extended binding interface with m4E-BPs, with significant implications on the understanding of translation regulation and the design of therapeutic molecules. Here we show the high-resolution structure of melon ( Cucumis melo ) eIF4E in complex with a melon eIF4G peptide and propose the first eIF4E-eIF4G structural model for plants. Our structural data together with functional analyses demonstrate that plant eIF4G binds to eIF4E through both the canonical and noncanonical motifs, similarly to metazoan eIF4E-eIF4G complexes. As in the case of metazoan eIF4E-eIF4G, this may have very important practical implications, as plant eIF4E-eIF4G is also involved in a significant number of plant diseases. In light of our results, a universal eukaryotic bipartite mode of binding to eIF4E is proposed.