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

22.7K
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...
22.7K
tRNA Activation02:26

tRNA Activation

8.4K
8.4K
lncRNA - Long Non-coding RNAs02:39

lncRNA - Long Non-coding RNAs

9.8K
In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding RNAs which includes ribosomal RNAs, transfer RNAs, telomerase RNAs, and regulatory RNAs, among other types. A large number of regulatory non-coding RNAs have been classified into two groups depending upon their length – small non-coding RNAs, such as microRNA, which are less than 200 nucleotides in length, and long non-coding RNA...
9.8K
Histone Modification02:32

Histone Modification

16.0K
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...
16.0K
Formal Charges02:42

Formal Charges

40.2K
In some cases, there are seemingly more than one valid Lewis structures for molecules and polyatomic ions. The concept of formal charges can be used to help predict the most appropriate Lewis structure when more than one reasonable structure exists.
40.2K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.4K
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...
9.4K

You might also read

Related Articles

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

Sort by
Same author

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

EMBO reports·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

Influence of total electron dose on the quality of nucleic acids potential maps in Cryo-EM.

Ultramicroscopy·2026
Same author

Activation of phosphoenolpyruvate carboxykinase increases intracellular glucose levels in podocytes under hyperglycemic conditions.

Biochimica et biophysica acta. Molecular cell research·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
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Related Experiment Video

Updated: Jan 24, 2026

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

12.8K

Charging the code - tRNA modification complexes.

Rościsław Krutyhołowa1, Karol Zakrzewski2, Sebastian Glatt3

  • 1Max Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland; Department of Cell Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Poland.

Current Opinion in Structural Biology
|May 19, 2019
PubMed
Summary
This summary is machine-generated.

Cellular RNA modifications, known as the epitranscriptome, are crucial for protein synthesis. This review details recent advances in understanding eukaryotic transfer RNA (tRNA) modifiers and their structures.

More Related Videos

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
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

14.7K

Related Experiment Videos

Last Updated: Jan 24, 2026

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

12.8K
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
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

14.7K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Cellular RNAs undergo post-transcriptional modifications, forming the epitranscriptome.
  • Transfer RNAs (tRNAs) are key modification sites, influencing translation.
  • Dysfunctional tRNA modification is linked to human diseases.

Purpose of the Study:

  • To review recent scientific progress in epitranscriptomics.
  • To summarize structural information of eukaryotic tRNA modifiers.

Main Methods:

  • Literature review of recent scientific publications.
  • Analysis of structural data for tRNA modifiers.

Main Results:

  • Eukaryotic tRNA modifiers are diverse and essential for cellular function.
  • Structural insights reveal mechanisms of tRNA modification.
  • Recent advances have expanded our understanding of these complexes.

Conclusions:

  • Epitranscriptomic modifications, particularly on tRNAs, are vital for proteome stability.
  • Structural studies of tRNA modifiers are critical for understanding their function and disease relevance.