eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation

被引：0
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作者：
Martin D. Jennings
Graham D. Pavitt
机构：
[1] Faculty of Life Sciences,
[2] University of Manchester,undefined
[3] Michael Smith Building,undefined
[4] Oxford Road,undefined
[5] Manchester M13 9PT,undefined
[6] UK ,undefined
来源：
Nature | 2010年 / 465卷
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摘要：
The translation factor that helps deliver the initiator tRNA to the ribosome, eIF2, uses the energy of GTP hydrolysis for function. Another factor, eIF5, was known to accelerate the GTPase activity of eIF2 when it was bound to the initiator tRNA and the ribosome. In this study two other roles for eIF5 have been defined. One involves stabilizing the binding of GDP, the product of GTP hydrolysis, to eIF2. The other involves its acting with phosphorylated eIF2 to inhibit the guanine nucleotide exchange factor, eIF2B. These results clarify our understanding of how translation initiation is regulated.
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页码：378 / 381
页数：3
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