DOI: 10.1073/pnas.1116821108. Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)

Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)

10.1073/pnas.1116821108

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Protein fate in higher eukaryotes is controlled by three complexes that share conserved architectural elements: the proteasome, COP9 signalosome, and eukaryotic translation initiation factor 3 (eIF3). Here we reconstitute the 13-subunit human eIF3 in Escherichia coli , revealing its structural core to be the eight subunits with conserved orthologues in the proteasome lid complex and COP9 signalosome. This structural core in eIF3 binds to the small (40S) ribosomal subunit, to translation initiation factors involved in mRNA cap-dependent initiation, and to the hepatitis C viral (HCV) internal ribosome entry site (IRES) RNA. Addition of the remaining eIF3 subunits enables reconstituted eIF3 to assemble intact initiation complexes with the HCV IRES. Negative-stain EM reconstructions of reconstituted eIF3 further reveal how the approximately 400 kDa molecular mass structural core organizes the highly flexible 800 kDa molecular mass eIF3 complex, and mediates translation initiation.

Bibliography

Sun, C., Todorovic, A., Querol-AudÃ, J., Bai, Y., Villa, N., Snyder, M., Ashchyan, J., Lewis, C. S., Hartland, A., Gradia, S., Fraser, C. S., Doudna, J. A., Nogales, E., & Cate, J. H. D. (2011). Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3). Proceedings of the National Academy of Sciences, 108(51), 20473â20478.

Authors 14

Chaomin Sun (first)
Aleksandar Todorovic (additional)
Jordi Querol-Audí (additional)
Yun Bai (additional)
Nancy Villa (additional)
Monica Snyder (additional)
John Ashchyan (additional)
Christopher S. Lewis (additional)
Abbey Hartland (additional)
Scott Gradia (additional)
Christopher S. Fraser (additional)
Jennifer A. Doudna (additional)
Eva Nogales (additional)
Jamie H. D. Cate (additional)

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Dates

Type	When
Created	13 years, 8 months ago (Dec. 3, 2011, 1:06 a.m.)
Deposited	3 years, 2 months ago (June 7, 2022, 4:19 a.m.)
Indexed	5 months ago (March 22, 2025, 5:30 a.m.)
Issued	13 years, 8 months ago (Dec. 1, 2011)
Published	13 years, 8 months ago (Dec. 1, 2011)
Published Online	13 years, 8 months ago (Dec. 1, 2011)
Published Print	13 years, 8 months ago (Dec. 20, 2011)

Funders 0

None

BibTeX

@article{Sun_2011, title={Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)}, volume={108}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.1116821108}, DOI={10.1073/pnas.1116821108}, number={51}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Sun, Chaomin and Todorovic, Aleksandar and Querol-Audí, Jordi and Bai, Yun and Villa, Nancy and Snyder, Monica and Ashchyan, John and Lewis, Christopher S. and Hartland, Abbey and Gradia, Scott and Fraser, Christopher S. and Doudna, Jennifer A. and Nogales, Eva and Cate, Jamie H. D.}, year={2011}, month=dec, pages={20473–20478} }

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  "abstract": "<jats:p>\n            Protein fate in higher eukaryotes is controlled by three complexes that share conserved architectural elements: the proteasome, COP9 signalosome, and eukaryotic translation initiation factor 3 (eIF3). Here we reconstitute the 13-subunit human eIF3 in\n            <jats:italic>Escherichia coli</jats:italic>\n            , revealing its structural core to be the eight subunits with conserved orthologues in the proteasome lid complex and COP9 signalosome. This structural core in eIF3 binds to the small (40S) ribosomal subunit, to translation initiation factors involved in mRNA cap-dependent initiation, and to the hepatitis C viral (HCV) internal ribosome entry site (IRES) RNA. Addition of the remaining eIF3 subunits enables reconstituted eIF3 to assemble intact initiation complexes with the HCV IRES. Negative-stain EM reconstructions of reconstituted eIF3 further reveal how the approximately 400\u00a0kDa molecular mass structural core organizes the highly flexible 800\u00a0kDa molecular mass eIF3 complex, and mediates translation initiation.\n          </jats:p>",
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