Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex

Jan P. Erzberger, Florian Stengel, Riccardo Pellarin, Suyang Zhang, Tanja Schaefer, Christopher H.S. Aylett, Peter Cimermančič, Daniel Boehringer, Andrej Sali, Ruedi Aebersold, Nenad Ban

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40SâeIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.

Original languageEnglish (US)
Pages (from-to)1123-1135
Number of pages13
JournalCell
Volume158
Issue number5
DOIs
StatePublished - Aug 28 2014

Fingerprint

Eukaryotic Small Ribosome Subunits
Multiprotein Complexes
Peptide Initiation Factors
Hepatitis C
Yeast
Saccharomyces cerevisiae
Mass Spectrometry
Electron Microscopy
Yeasts
X-Rays
RNA
Messenger RNA
Clamping devices
Electron microscopy
Machinery
Mass spectrometry
X rays

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Erzberger, J. P., Stengel, F., Pellarin, R., Zhang, S., Schaefer, T., Aylett, C. H. S., ... Ban, N. (2014). Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex. Cell, 158(5), 1123-1135. https://doi.org/10.1016/j.cell.2014.07.044

Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex. / Erzberger, Jan P.; Stengel, Florian; Pellarin, Riccardo; Zhang, Suyang; Schaefer, Tanja; Aylett, Christopher H.S.; Cimermančič, Peter; Boehringer, Daniel; Sali, Andrej; Aebersold, Ruedi; Ban, Nenad.

In: Cell, Vol. 158, No. 5, 28.08.2014, p. 1123-1135.

Research output: Contribution to journalArticle

Erzberger, JP, Stengel, F, Pellarin, R, Zhang, S, Schaefer, T, Aylett, CHS, Cimermančič, P, Boehringer, D, Sali, A, Aebersold, R & Ban, N 2014, 'Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex', Cell, vol. 158, no. 5, pp. 1123-1135. https://doi.org/10.1016/j.cell.2014.07.044
Erzberger JP, Stengel F, Pellarin R, Zhang S, Schaefer T, Aylett CHS et al. Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex. Cell. 2014 Aug 28;158(5):1123-1135. https://doi.org/10.1016/j.cell.2014.07.044
Erzberger, Jan P. ; Stengel, Florian ; Pellarin, Riccardo ; Zhang, Suyang ; Schaefer, Tanja ; Aylett, Christopher H.S. ; Cimermančič, Peter ; Boehringer, Daniel ; Sali, Andrej ; Aebersold, Ruedi ; Ban, Nenad. / Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex. In: Cell. 2014 ; Vol. 158, No. 5. pp. 1123-1135.
@article{8994d12c40314221beeb8f5ebee40efb,
title = "Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex",
abstract = "Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40S{\^a}eIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.",
author = "Erzberger, {Jan P.} and Florian Stengel and Riccardo Pellarin and Suyang Zhang and Tanja Schaefer and Aylett, {Christopher H.S.} and Peter Cimermančič and Daniel Boehringer and Andrej Sali and Ruedi Aebersold and Nenad Ban",
year = "2014",
month = "8",
day = "28",
doi = "10.1016/j.cell.2014.07.044",
language = "English (US)",
volume = "158",
pages = "1123--1135",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - Molecular architecture of the 40S · eIF1 · eIF3 translation initiation complex

AU - Erzberger, Jan P.

AU - Stengel, Florian

AU - Pellarin, Riccardo

AU - Zhang, Suyang

AU - Schaefer, Tanja

AU - Aylett, Christopher H.S.

AU - Cimermančič, Peter

AU - Boehringer, Daniel

AU - Sali, Andrej

AU - Aebersold, Ruedi

AU - Ban, Nenad

PY - 2014/8/28

Y1 - 2014/8/28

N2 - Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40SâeIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.

AB - Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40SâeIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.

UR - http://www.scopus.com/inward/record.url?scp=84907323467&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84907323467&partnerID=8YFLogxK

U2 - 10.1016/j.cell.2014.07.044

DO - 10.1016/j.cell.2014.07.044

M3 - Article

VL - 158

SP - 1123

EP - 1135

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

ER -