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

Translation01:31

Translation

157.1K
Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
157.1K
Translation01:31

Translation

17.9K
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Proteins are...
17.9K
Initiation of Translation02:33

Initiation of Translation

39.1K
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...
39.1K
Termination of Translation01:44

Termination of Translation

27.8K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
27.8K
Improving Translational Accuracy02:07

Improving Translational Accuracy

15.0K
Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
15.0K
Histone Modification02:32

Histone Modification

16.2K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.2K

You might also read

Related Articles

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

Sort by
Same author

Frequency and risk factors for symptomatic pulmonary embolism following spinal fusion surgery exceeding 6 hours: dynamic risk stratification using a two-stage predictive model.

The spine journal : official journal of the North American Spine Society·2026
Same author

Template guided versus freehand rod bending in spinal deformity surgery: a feasibility study.

Scientific reports·2026
Same author

Evaluation of HIV-1 drug resistance in newly diagnosed individuals in Italy over the period 2017-2023.

Journal of global antimicrobial resistance·2025
Same author

Cutaneous diphtheria in a child returning from visiting friends & relatives in Burkina Faso: a case report.

Infection·2025
Same author

Intermediate dose enoxaparin in hospitalized patients with moderate-severe COVID-19: a pilot phase II single-arm study, INHIXACOVID19.

BMC infectious diseases·2023
Same author

Predictive comorbidities of hospital admission in 1,571 SARS- CoV-2 positive patients: analysis of administrative data from an Italian Local Health Autority.

La Clinica terapeutica·2022

Related Experiment Video

Updated: Feb 7, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.6K

Modification of translation factor aIF5A from Sulfolobus solfataricus.

F Bassani1, A Romagnoli1, T Cacciamani1,2

  • 1Department of Life and Environmental Sciences, Polytechnic University of Marche, Via Brecce Bianche, 60131, Ancona, Italy.

Extremophiles : Life Under Extreme Conditions
|July 27, 2018
PubMed
Summary

Archaea possess a translation elongation factor, aIF5A, which is hypusinated. This study identifies its interaction with deoxyhypusine synthase, clarifying a key step in its essential post-translational modification.

Keywords:
Deoxyhypusine synthaseHypusinationPost-translational modificationSulfolobus solfataricusTranslation factor aIF5A

More Related Videos

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
10:12

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

3.7K
Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
10:26

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

6.1K

Related Experiment Videos

Last Updated: Feb 7, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.6K
Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
10:12

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

3.7K
Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
10:26

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

6.1K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Eukaryotic eIF5A and bacterial EF-P are translation factors crucial for protein synthesis, preventing ribosome stalling.
  • These factors require specific post-translational modifications (hypusination and lysinylation) for function.
  • Archaea have an orthologue, but its function and modification remain largely unknown.

Purpose of the Study:

  • To investigate the function and post-translational modification of the archaeal translation factor aIF5A from Sulfolobus solfataricus.
  • To identify the enzymes involved in the hypusination pathway of aIF5A.

Main Methods:

  • Characterization of aIF5A from Sulfolobus solfataricus.
  • Biochemical assays using recombinant deoxyhypusine synthase.
  • Identification of interacting proteins with aIF5A.

Main Results:

  • Sulfolobus solfataricus aIF5A undergoes hypusination.
  • aIF5A forms a stable complex with deoxyhypusine synthase.
  • Recombinant deoxyhypusine synthase successfully modifies aIF5A in vitro.
  • Proteins interacting with aIF5A were identified to elucidate the second modification step.

Conclusions:

  • The study confirms hypusination of archaeal aIF5A and its interaction with deoxyhypusine synthase.
  • This provides insight into the functional mechanism of aIF5A in Archaea.
  • Further research will identify the enzyme responsible for the complete hypusination process.