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

Transfer RNA Synthesis02:36

Transfer RNA Synthesis

12.8K
One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
12.8K
Transfer RNA Synthesis02:35

Transfer RNA Synthesis

3.3K
3.3K
tRNA Activation02:26

tRNA Activation

21.6K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
21.6K
tRNA Activation02:26

tRNA Activation

7.9K
7.9K
Transcription Elongation Factors02:35

Transcription Elongation Factors

12.4K
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...
12.4K
Transcription Elongation Factors02:35

Transcription Elongation Factors

4.3K
4.3K

You might also read

Related Articles

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

Sort by
Same author

The impact of psuedouridine modification on human tRNA.

Biochemical Society transactions·2026
Same author

The EF-hand domain of MINDY3 is a ubiquitin and RAD23 UBL-binding domain.

EMBO reports·2026
Same author

Tools For Building Artificial Biological Nanostructures.

ACS nano·2026
Same author

Structure-Guided Discovery of OAT-4828 as Potent, Selective, and Orally Bioavailable USP7 Inhibitor with <i>In Vivo</i> Antileukemic Activity.

Journal of medicinal chemistry·2026
Same author

Structural insights into the Urm1-Uba4 pathway and its biological roles.

Essays in biochemistry·2026
Same author

Solid-state nanopore sensing reveals conformational changes induced by a mutation in a neuron-specific tRNAArg.

Nucleic acids research·2026

Related Experiment Video

Updated: Dec 2, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.3K

How Elongator Acetylates tRNA Bases.

Nour-El-Hana Abbassi1,2, Anna Biela1, Sebastian Glatt1

  • 1Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, Poland.

International Journal of Molecular Sciences
|November 6, 2020
PubMed
Summary
This summary is machine-generated.

Elp3, a key enzyme in tRNA modification, links acetyl-CoA metabolism to protein synthesis. Its dysregulation is implicated in human diseases like cancer and neurodegeneration.

Keywords:
ElongatorElp3acetyl-CoAcancersneurodegenerative diseasesproteome balancetRNA modification

More Related Videos

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

10.0K
Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.3K

Related Experiment Videos

Last Updated: Dec 2, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.3K
Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
10:59

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

10.0K
Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Elp3 is the catalytic subunit of the eukaryotic Elongator complex.
  • Elp3 functions as a lysine acetyltransferase, modifying transfer RNAs (tRNAs).
  • This modification occurs at the C5 position of wobble-base uridines (U34) in tRNAs.

Purpose of the Study:

  • To review recent findings on the structure of Elp3.
  • To elucidate the role of acetyl-CoA in the Elp3-mediated tRNA modification reaction.
  • To highlight the link between Elp3 activity, protein synthesis, and human diseases.

Main Methods:

  • Structural analysis of Elp3.
  • Biochemical assays to study Elp3 activity.
  • Review of existing literature on Elp3 function and disease association.

Main Results:

  • Recent structural insights into Elp3 provide a basis for understanding its catalytic mechanism.
  • Acetyl-CoA is crucial for Elp3's unique RNA acetylation reaction.
  • Elp3-dependent tRNA acetylation impacts ribosomal translation elongation rates.

Conclusions:

  • Elp3-mediated tRNA modification is a critical link between acetyl-CoA metabolism and protein synthesis.
  • Dysregulation of Elp3's tRNA modification activity is associated with human diseases, including cancers and neurodegenerative disorders.
  • Further research into Elp3 structure and function may offer therapeutic targets for related diseases.