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The chaperonin CCT interacts with and mediates the correct folding and activity of three subunits of translation initiation factor eIF3: b, i and h

Roobol, Anne, Roobol, Joanne, Carden, Martin J., Smith, Matthew E., Hershey, John W. B., Bastide, Amandine, Knight, John R. P., Willis, Anne E., Smales, Christopher Mark (2014) The chaperonin CCT interacts with and mediates the correct folding and activity of three subunits of translation initiation factor eIF3: b, i and h. Biochemical Journal, 458 (2). pp. 213-224. ISSN 0264-6021. (doi:10.1042/BJ20130979) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:38990)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1042/BJ20130979

Abstract

eIF3 (eukaryotic initiation factor 3) is the largest and most complex eukaryotic mRNA translation factor in terms of the number of protein components or subunits. In mammals, eIF3 is composed of 13 different polypeptide subunits, of which five, i.e. a, b, c, g and i, are conserved and essential in vivo from yeasts to mammals. In the present study, we show that the eukaryotic cytosolic chaperonin CCT [chaperonin containing TCP-1 (tailless complex polypeptide 1)] binds to newly synthesized eIF3b and promotes the correct folding of eIF3h and eIF3i. Interestingly, overexpression of these last two subunits is associated with enhanced translation of specific mRNAs over and above the general enhancement of global translation. In agreement with this, our data show that, as CCT is required for the correct folding of eIF3h and eIF3i subunits, it indirectly influences gene expression with eIF3i overexpression enhancing both cap- and IRES (internal ribosome entry segment)-dependent translation initiation, whereas eIF3h overexpression selectively increases IRES-dependent translation initiation. Importantly, these studies demonstrate the requirement of the chaperonin machinery for the correct folding of essential components of the translational machinery and provide further evidence of the close interplay between the cell environment, cell signalling, cell proliferation, the chaperone machinery and translational apparatus.

Item Type: Article
DOI/Identification number: 10.1042/BJ20130979
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Mark Smales
Date Deposited: 01 Apr 2014 13:13 UTC
Last Modified: 17 Aug 2022 10:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/38990 (The current URI for this page, for reference purposes)

University of Kent Author Information

Roobol, Anne.

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CReDIT Contributor Roles:

Roobol, Joanne.

Creator's ORCID:
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Carden, Martin J..

Creator's ORCID:
CReDIT Contributor Roles:

Smales, Christopher Mark.

Creator's ORCID: https://orcid.org/0000-0002-2762-4724
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