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Identification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complex

Identification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complex
Identification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complex
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.
protein domains, protein self-assembly, protein synthesis, translation, translation initiation factors, I-patch, eIF2B
0021-9258
8263-8274
Wang, Xuemin
d6bb4eb2-5687-46ed-b770-cceb22fd792e
Wortham, Noel C.
9b0a219d-41fa-4f83-9621-6ffd60f44c8f
Liu, Rui
f6ba8ec9-4057-4dd9-a960-d63f660eee09
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
Wang, Xuemin
d6bb4eb2-5687-46ed-b770-cceb22fd792e
Wortham, Noel C.
9b0a219d-41fa-4f83-9621-6ffd60f44c8f
Liu, Rui
f6ba8ec9-4057-4dd9-a960-d63f660eee09
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3

Wang, Xuemin, Wortham, Noel C., Liu, Rui and Proud, Christopher G. (2012) Identification of residues that underpin interactions within the eukaryotic initiation factor (eIF2) 2B complex. The Journal of Biological Chemistry, 287 (11), 8263-8274. (doi:10.1074/jbc.M111.331553). (PMID:22238342)

Record type: Article

Abstract

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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More information

Published date: 9 March 2012
Keywords: protein domains, protein self-assembly, protein synthesis, translation, translation initiation factors, I-patch, eIF2B
Organisations: Molecular and Cellular

Identifiers

Local EPrints ID: 337177
URI: http://eprints.soton.ac.uk/id/eprint/337177
ISSN: 0021-9258
PURE UUID: 2267baca-49a9-4523-8268-ddccf4343be1

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Date deposited: 20 Apr 2012 10:10
Last modified: 14 Mar 2024 10:50

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Contributors

Author: Xuemin Wang
Author: Noel C. Wortham
Author: Rui Liu
Author: Christopher G. Proud

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