Skip to Content

The three-dimensional arcitecture of the EJC core

TitleThe three-dimensional arcitecture of the EJC core
Publication TypeJournal Article
Year of Publication2006
AuthorsStroupe, ME, Tange TO, Thomas DR, Moore MJ, Grigorieff N
Refereed DesignationRefereed
JournalJ Mol Biol
Date PublishedJul 21
ISBN Number0022-2836 (Print)
Accession Number16797590
Keywords*Exons, *RNA Splice Sites, Crystallography, X-Ray, Eukaryotic Initiation Factor-4A/chemistry/metabolism, Gene Expression, Humans, Models, Molecular, Negative Staining, Neoplasm Proteins/chemistry/ultrastructure, Nuclear Proteins/chemistry/ultrastructure, Protein Binding, purification/*metabolism/ultrastructure, Ribonucleoproteins/*chemistry/isolation &

The exon junction complex (EJC) is a macromolecular complex deposited at splice junctions on mRNAs as a consequence of splicing. At the core of the EJC are four proteins: eIF4AIII, a member of the DExH/D-box family of NTP-dependent RNA binding proteins, Y14, Magoh, and MLN51. These proteins form a stable heterotetramer that remains bound to the mRNA throughout many different cellular environments. We have determined the three-dimensional (3D) structure of this EJC core using negative-stain random-conical tilt electron microscopy. This structure represents the first structure of a DExH/D-box protein in complex with its binding partners. The EJC core is a four-lobed complex with a central channel and dimensions consistent with its known RNA footprint of about ten nucleotides. Using known X-ray crystallographic structures and a model of three of the four components, we propose a model for complex assembly on RNA and explain how Y14:Magoh may influence eIF4AIII's RNA binding.

Stroupe_JMB2006.pdf348.38 KB