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.
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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 -