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Initiation of Translation

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...

Initiation of Translation

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...

General Transcription Factors

General Transcription Factors

Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Transcription Elongation Factors

Transcription Elongation Factors

Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...

Transcription Elongation Factors

Transcription Elongation Factors

Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA into a...

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Related Experiment Video

Updated: Jul 10, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

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Published on: May 1, 2020

Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and

Mikhail Reibarkh¹, Yasufumi Yamamoto, Chingakham Ranjit Singh

¹Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

The Journal of Biological Chemistry

|November 3, 2007

Summary

This summary is machine-generated.

Eukaryotic initiation factor 1 (eIF1) interacts with eIF5 at a novel site, crucial for accurate translation start codon selection. This interaction ensures proper assembly of the translation initiation complex and prevents premature eIF1 release.

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Area of Science:

Molecular Biology
Protein-Protein Interactions
Translation Regulation

Background:

Eukaryotic initiation factor 1 (eIF1) is essential for accurate translation initiation fidelity.
eIF1 functions within a large multifactor complex on the 40S ribosomal subunit.
The precise interfaces of eIF1 with other initiation factors, particularly eIF5, remain largely uncharacterized.

Purpose of the Study:

To identify the binding site of eIF5 on eIF1.
To elucidate the functional significance of the eIF1-eIF5 interaction in translation initiation.
To understand how this interaction contributes to start codon selection fidelity.

Main Methods:

Solution structure determination of yeast eIF1.
Identification of eIF5 binding site on eIF1 using structural and biochemical approaches.
Genetic analysis of eIF1 mutations affecting start codon selection.

Main Results:

The N-terminal tail and KH domain of eIF1 form the binding site for eIF5, distinct from the ribosome-binding face.
The eIF1 N-terminal tail promotes cooperative multifactor assembly.
A mutation in the eIF1 KH domain's basic region is lethal and causes relaxed start codon selection, implicating this site in fidelity.
eIF5 is proposed as the direct partner of eIF1-KH, mediating a critical link for regulated eIF1 release.

Conclusions:

The eIF1-eIF5 interaction occurs at a novel site (eIF1-KH) and is critical for translation initiation fidelity.
This interaction likely stabilizes the preinitiation complex and ensures accurate start codon recognition.
Understanding this interface provides insights into the molecular mechanisms governing translation initiation regulation.