Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Initiation of Translation02:33

Initiation of Translation

24.7K
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...
24.7K
Initiation of Translation02:33

Initiation of Translation

7.0K
7.0K
Transcription Elongation Factors02:35

Transcription Elongation Factors

11.2K
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...
11.2K
Transcription Elongation Factors02:35

Transcription Elongation Factors

3.8K
3.8K
Leaky Scanning02:28

Leaky Scanning

4.5K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
4.5K
General Transcription Factors01:30

General Transcription Factors

5.9K
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...
5.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Short- and long-term changes in renal function following percutaneous cryoablation: a comparison of endophytic versus exophytic renal tumors.

Journal of vascular and interventional radiology : JVIR·2026
Same author

TGFb signaling instructs a conserved fibrosis-associated cell state marked by LRRC15.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

A Phosphorylation Switch Modulates Configurational Codes in the Oncofetal IGF2BP RNA Binding Paralogs.

bioRxiv : the preprint server for biology·2026
Same author

Distribution-preserved sampling (DPS) for smarter machine learning assisted ultra-large-scale virtual screening.

RSC advances·2026
Same author

AI-Enhanced Adaptive Virtual Screening Platform Enabling Exploration of 69 Billion Molecules Discovers Structurally Validated FSP1 Inhibitors.

bioRxiv : the preprint server for biology·2026
Same author

Interrupted Inferior Vena Cava and Duplicated Superior Vena Cavae Identified During Catheter Ablation.

JACC. Case reports·2026

Related Experiment Video

Updated: May 5, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

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

Published on: May 1, 2020

2.5K

The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation

Rafael E Luna1, Haribabu Arthanari, Hiroyuki Hiraishi

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

Biochemistry
|December 11, 2013
PubMed
Summary
This summary is machine-generated.

Eukaryotic initiation factor 1A (eIF1A) binds to eIF5

More Related Videos

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.1K
Xenopus laevis as a Model to Identify Translation Impairment
10:24

Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

10.3K

Related Experiment Videos

Last Updated: May 5, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

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

Published on: May 1, 2020

2.5K
Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells

Published on: December 25, 2021

4.1K
Xenopus laevis as a Model to Identify Translation Impairment
10:24

Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

10.3K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Scanning the mRNA transcript by the preinitiation complex (PIC) requires eukaryotic initiation factors.
  • eIF1A is crucial for start codon recognition, but its interaction with eIF5 is not understood.

Purpose of the Study:

  • To elucidate the molecular interaction between eIF1A and eIF5.
  • To identify the binding surface and mediating regions for this interaction.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy to map binding surfaces.
  • Mutational analysis of eIF5-CTD.
  • Glutathione S-transferase (GST) pull-down assays.
  • Genetic analysis of eIF1A mutants.

Main Results:

  • NMR revealed eIF1A's binding surface on the carboxyl-terminal domain of eIF5 (eIF5-CTD).
  • The N-terminal tail (NTT) of eIF1A mediates binding to eIF5-CTD and eIF1.
  • This interaction is conserved between humans and yeast.
  • Overexpression of eIF1 or eIF5 suppressed the growth defects of eIF1A-NTT mutants.

Conclusions:

  • The eIF1A-eIF5-CTD interaction is essential for maintaining eIF1 within the open PIC during mRNA scanning.
  • This interaction plays a role in stringent AUG selection during translation initiation.