【字体: 时间:2009年05月13日 来源:Nature


  生物通报道,美国NIH以及Johns Hopkins医学院的研究者在蛋白延伸因子方面的研究取得新的进展,为蛋白翻译延伸因子调节蛋白翻译的研究打开了新的视野,文章标题Hypusine-containing protein eIF5A promotes translation elongation。


生物通报道,美国NIH以及Johns Hopkins医学院的研究者在蛋白延伸因子方面的研究取得新的进展,为蛋白翻译延伸因子调节蛋白翻译的研究打开了新的视野,文章标题Hypusine-containing protein eIF5A promotes translation elongation







(生物通 小茜)


生物通推荐原文检索:Hypusine-containing protein eIF5A promotes translation elongation

Preeti Saini1, Daniel E. Eyler2, Rachel Green2 & Thomas E. Dever1


Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA

Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA




Top of pageTranslation elongation factors facilitate protein synthesis by the ribosome. Previous studies identified two universally conserved translation elongation factors, EF-Tu in bacteria (known as eEF1A in eukaryotes) and EF-G (eEF2), which deliver aminoacyl-tRNAs to the ribosome and promote ribosomal translocation, respectively1. The factor eIF5A (encoded by HYP2 and ANB1 in Saccharomyces cerevisiae), the sole protein in eukaryotes and archaea to contain the unusual amino acid hypusine (N -(4-amino-2-hydroxybutyl)lysine)2, was originally identified based on its ability to stimulate the yield (endpoint) of methionyl-puromycin synthesis—a model assay for first peptide bond synthesis thought to report on certain aspects of translation initiation3, 4. Hypusine is required for eIF5A to associate with ribosomes5, 6 and to stimulate methionyl-puromycin synthesis7. Because eIF5A did not stimulate earlier steps of translation initiation8, and depletion of eIF5A in yeast only modestly impaired protein synthesis9, it was proposed that eIF5A function was limited to stimulating synthesis of the first peptide bond or that eIF5A functioned on only a subset of cellular messenger RNAs. However, the precise cellular role of eIF5A is unknown, and the protein has also been linked to mRNA decay, including the nonsense-mediated mRNA decay pathway10, 11, and to nucleocytoplasmic transport12, 13. Here we use molecular genetic and biochemical studies to show that eIF5A promotes translation elongation. Depletion or inactivation of eIF5A in the yeast S. cerevisiae resulted in the accumulation of polysomes and an increase in ribosomal transit times. Addition of recombinant eIF5A from yeast, but not a derivative lacking hypusine, enhanced the rate of tripeptide synthesis in vitro. Moreover, inactivation of eIF5A mimicked the effects of the eEF2 inhibitor sordarin, indicating that eIF5A might function together with eEF2 to promote ribosomal translocation. Because eIF5A is a structural homologue of the bacterial protein EF-P14, 15, we propose that eIF5A/EF-P is a universally conserved translation elongation factor.

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