Molecular biology: Structural roles for human translation factor elF3 in initiation of protein synthesis

Bunpote Siridechadilok, Christopher S. Fraser, Richard J. Hall, Jennifer A. Doudna, Eva Nogales

Research output: Contribution to journal › Article

212 Citations (Scopus)

Abstract

Protein synthesis in mammalian cells requires initiation factor elF3, a ∼750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5′-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that elF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5′-cap binding complex elF4F via the same domain. Detailed modeling of elF3 and elF4F onto the 40S ribosomal subunit reveals that elF3 uses elF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.

Original languageEnglish (US)
Pages (from-to)1513-1515
Number of pages3
JournalScience
Volume310
Issue number5753
DOIs
StatePublished - Dec 2 2005

Fingerprint

Eukaryotic Small Ribosome Subunits
Molecular Biology
Hepacivirus
RNA Caps
Cryoelectron Microscopy
Peptide Initiation Factors
Messenger RNA
Proteins
Internal Ribosome Entry Sites

ASJC Scopus subject areas

  • General

Cite this

Siridechadilok, B., Fraser, C. S., Hall, R. J., Doudna, J. A., & Nogales, E. (2005). Molecular biology: Structural roles for human translation factor elF3 in initiation of protein synthesis. Science, 310(5753), 1513-1515. https://doi.org/10.1126/science.1118977

Molecular biology : Structural roles for human translation factor elF3 in initiation of protein synthesis. / Siridechadilok, Bunpote; Fraser, Christopher S.; Hall, Richard J.; Doudna, Jennifer A.; Nogales, Eva.

In: Science, Vol. 310, No. 5753, 02.12.2005, p. 1513-1515.

Research output: Contribution to journal › Article

Siridechadilok, B, Fraser, CS, Hall, RJ, Doudna, JA & Nogales, E 2005, 'Molecular biology: Structural roles for human translation factor elF3 in initiation of protein synthesis', Science, vol. 310, no. 5753, pp. 1513-1515. https://doi.org/10.1126/science.1118977
Siridechadilok B, Fraser CS, Hall RJ, Doudna JA, Nogales E. Molecular biology: Structural roles for human translation factor elF3 in initiation of protein synthesis. Science. 2005 Dec 2;310(5753):1513-1515. https://doi.org/10.1126/science.1118977
Siridechadilok, Bunpote ; Fraser, Christopher S. ; Hall, Richard J. ; Doudna, Jennifer A. ; Nogales, Eva. / Molecular biology : Structural roles for human translation factor elF3 in initiation of protein synthesis. In: Science. 2005 ; Vol. 310, No. 5753. pp. 1513-1515.
@article{0122588a0c3949cf86883c08b833d20a,
title = "Molecular biology: Structural roles for human translation factor elF3 in initiation of protein synthesis",
abstract = "Protein synthesis in mammalian cells requires initiation factor elF3, a ∼750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5′-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that elF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5′-cap binding complex elF4F via the same domain. Detailed modeling of elF3 and elF4F onto the 40S ribosomal subunit reveals that elF3 uses elF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.",
author = "Bunpote Siridechadilok and Fraser, {Christopher S.} and Hall, {Richard J.} and Doudna, {Jennifer A.} and Eva Nogales",
year = "2005",
month = "12",
day = "2",
doi = "10.1126/science.1118977",
language = "English (US)",
volume = "310",
pages = "1513--1515",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5753",

}

TY - JOUR

T1 - Molecular biology

T2 - Structural roles for human translation factor elF3 in initiation of protein synthesis

AU - Siridechadilok, Bunpote

AU - Fraser, Christopher S.

AU - Hall, Richard J.

AU - Doudna, Jennifer A.

AU - Nogales, Eva

PY - 2005/12/2

Y1 - 2005/12/2

N2 - Protein synthesis in mammalian cells requires initiation factor elF3, a ∼750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5′-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that elF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5′-cap binding complex elF4F via the same domain. Detailed modeling of elF3 and elF4F onto the 40S ribosomal subunit reveals that elF3 uses elF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.

AB - Protein synthesis in mammalian cells requires initiation factor elF3, a ∼750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5′-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that elF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5′-cap binding complex elF4F via the same domain. Detailed modeling of elF3 and elF4F onto the 40S ribosomal subunit reveals that elF3 uses elF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.

UR - http://www.scopus.com/inward/record.url?scp=28544439977&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=28544439977&partnerID=8YFLogxK

U2 - 10.1126/science.1118977

DO - 10.1126/science.1118977

M3 - Article

C2 - 16322461

AN - SCOPUS:28544439977

VL - 310

SP - 1513

EP - 1515

JO - Science

JF - Science

SN - 0036-8075

IS - 5753

ER -

Access to Document