5me6
Crystal Structure of eiF4E from C. melo bound to a CAP analog
Structural highlights
FunctionIF4E1_CUCME Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:17026540, PubMed:28522457). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:17026540, PubMed:28522457). Key component of recessive resistance to potyviruses and Tombusviridae genus Carmovirus such as melon necrotic spot virus (MNSV) (PubMed:17026540).[1] [2] (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs, including uncapped and non-polyadenylated RNA, to the host ribosomal complex via an interaction with viral genome-linked protein (VPg).[3] Publication Abstract from PubMedThe 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. Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation.,Miras M, Truniger V, Silva C, Verdaguer N, Aranda MA, Querol-Audi J Plant Physiol. 2017 Jul;174(3):1476-1491. doi: 10.1104/pp.17.00193. Epub 2017 May, 18. PMID:28522457[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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