Wang, Xuemin, Wortham, Noel C., Liu, Rui and Proud, Christopher G.
Identification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complex
The Journal of Biological Chemistry, 287, (11), . (doi:10.1074/jbc.M111.331553). (PMID:22238342).
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Eukaryotic initiation factor 2B (eIF2B) plays a key role in protein synthesis an in its control. It comprises five different subunits, ?-?, of which eIF2B? contains the catalytic domain. Formation of the complete complex is crucial for full activity and proper control of eIF2B. Mutations in the genes for eIF2B cause an often-severe neurological disorder, vanishing white matter (VWM). eIF2B? and eIF2B? contain homologous and conserved domains with sequence similarity to nucleotidyltransferases (ITs) and acyltransferases and can form a binary complex. The latter contain a hexad repeat that mainly comprises isoleucyl residues (hence termed the I-patch region). The present data reveal that certain residues in the NT domains of eIF2B?/?, which are highly conserved throughout eukaryotes, play key roles in the interactions between subunits in the eIF2B complex. Our data show that the I-patch regions are important in the interactions between the catalytic eIF2B?? complex and the other subunits. We also study the functional effects of VWM mutations in the NT and I-patch domains. Lastly, our data show that eIF2B? promotes the expression of eIF2B?, providing a mechanism for achieving correct stoichiometry of these eIF2B subunits in the cell.
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