Abstract:
: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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Stroupe ME,Tange TØ,Thomas DR,Moore MJ,Grigorieff Ndoi
10.1016/j.jmb.2006.05.049subject
Has Abstractpub_date
2006-07-21 00:00:00pages
743-9issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(06)00650-4journal_volume
360pub_type
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