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PERSPECTIVE

Translation factor control of ribosome conformation during start codon selection

¹ Molecular Cellular and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, Kansas 66506, USA; ² Department of Environmental and Biomolecular Systems, Oregon Health and Science University, Beaverton, Oregon 97006, USA; ³ Department of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, Oregon 97201, USA

The first 100 words of the full text of this article appear below.

Eukaryotic translation initiation factors (eIFs) function at multiple steps. They enable the small 40S ribosome subunit to bind to initiator tRNA and mRNA, and scan to and select an initiation codon on the mRNA. They facilitate joining of the large 60S ribosome subunit, at which point the initiation phase of translation ends with the initiator tRNA in the P (peptidyl) site, and the ribosome poised to accept a tRNA into its A (aminoacyl) site (Kapp and Lorsch 2004; Pestova et al. 2007). There are at least 10 eIFs, and many of them (eIF1, eIF1A, eIF2, eIF3, eIF4F, eIF5, . . . [Full Text of this Article]

	An overview of yeast genetic studies on eIF functions

 

	eIF1 as a regulator of start site selection

 

	Evidence for eIF1 release as a critical checkpoint of start codon selection

 

	The eIF1-NTT promotes MFC assembly and regulates PIC function

 

	Tales of tails: roles of unstructured terminal tails in eukaryotic initiation

 

	Translational control by MFC

 

	Concluding remarks

 

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