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

tRNA Activation02:26

tRNA Activation

23.2K
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...
23.2K
tRNA Activation02:26

tRNA Activation

8.7K
8.7K
Transcription Elongation Factors02:35

Transcription Elongation Factors

14.1K
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...
14.1K
Transcription Elongation Factors02:35

Transcription Elongation Factors

4.9K
4.9K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.5K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
9.5K
Histone Modification02:32

Histone Modification

16.3K
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...
16.3K

You might also read

Related Articles

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

Sort by
Same author

The Motor Neuron Disease Register for England, Wales, and Northern Ireland: Protocol for a Population Register.

JMIR research protocols·2026
Same author

CYP2D6 variants in amyotrophic lateral sclerosis: an association study of risk and survival.

Brain : a journal of neurology·2026
Same author

Gut microbiota and ALS: cause, consequence or correlation? - a systematic review.

Frontiers in neuroscience·2026
Same author

Large-scale exome analyses reveal new rare variant contributions in amyotrophic lateral sclerosis.

Nature genetics·2026
Same author

The lipid transfer protein STARD7 controls intestinal tumor development in a context-dependent manner.

EMBO molecular medicine·2026
Same author

Digenic inheritance of mutations in SPG7 and AFG3L2 causes motor neuron and cerebellar disorders.

BMC medicine·2026

Related Experiment Video

Updated: Feb 14, 2026

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
07:46

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity

Published on: October 8, 2018

7.5K

Elongator subunit 3 (ELP3) modifies ALS through tRNA modification.

Andre Bento-Abreu1,2, Gunilla Jager3, Bart Swinnen1,2,4

  • 1Department of Neurosciences, Experimental Neurology and Leuven Institute for Neuroscience and Disease (LIND), KU Leuven-University of Leuven, B-3000 Leuven, Belgium.

Human Molecular Genetics
|February 8, 2018
PubMed
Summary
This summary is machine-generated.

ELP3, a tRNA modifying enzyme, was found to be a key modifier in amyotrophic lateral sclerosis (ALS). Its expression impacts neurodegeneration, suggesting a link between tRNA modification and ALS progression.

More Related Videos

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
12:36

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme

Published on: October 19, 2010

14.8K
Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays
07:32

Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays

Published on: June 18, 2010

12.9K

Related Experiment Videos

Last Updated: Feb 14, 2026

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
07:46

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity

Published on: October 8, 2018

7.5K
In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
12:36

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme

Published on: October 19, 2010

14.8K
Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays
07:32

Genome-wide Analysis of Aminoacylation Charging Levels of tRNA Using Microarrays

Published on: June 18, 2010

12.9K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease affecting motor neurons.
  • The progression of ALS is influenced by various disease-modifying factors.
  • The elongator complex subunit ELP3's role in ALS is not well understood.

Purpose of the Study:

  • To investigate ELP3 as a potential disease modifier in amyotrophic lateral sclerosis (ALS).
  • To explore the link between tRNA modification and neurodegeneration in ALS.

Main Methods:

  • Utilized zebrafish and mouse models of ALS (mutant SOD1 and C9orf72).
  • Assessed the impact of ELP3 expression on axonopathy, survival, and denervation.
  • Investigated ELP3's effect on tRNA wobble uridine modification (mcm5s2U) and mutant SOD1 aggregation in vitro.
  • Analyzed ELP3 expression levels in the motor cortex of ALS patients.

Main Results:

  • ELP3 attenuated axonopathy in mutant SOD1 and C9orf72 ALS zebrafish models.
  • Increased ELP3 expression in a SOD1G93A mouse model extended survival and reduced denervation.
  • ELP3 depletion in vitro decreased mcm5s2U levels and increased insoluble mutant SOD1, effects reversed by exogenous ELP3.
  • Reduced ELP3 expression and mcm5s2U levels were observed in the motor cortex of ALS patients.

Conclusions:

  • ELP3 acts as a significant modifier of ALS progression.
  • Findings suggest a novel connection between tRNA modification and the mechanisms underlying neurodegeneration in ALS.
  • ELP3 represents a potential therapeutic target for ALS.