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

Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

26.8K
RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
26.8K
RNA Editing02:23

RNA Editing

9.8K
RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
9.8K
tRNA Activation02:26

tRNA Activation

22.6K
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...
22.6K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.5K
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
32.5K
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

13.2K
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...
13.2K
Transcription Initiation01:47

Transcription Initiation

20.3K
Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
The promoters and enhancers and their accessory proteins allow tight regulation of...
20.3K

You might also read

Related Articles

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

Sort by
Same author

Structure of the NAT10 acetyltransferase and mechanism of tRNA acetylation.

Nature communications·2026
Same author

A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.

bioRxiv : the preprint server for biology·2026
Same author

Hierarchical small molecule inhibition of MYST acetyltransferases.

Nature communications·2026
Same author

Archaeal family B DNA polymerase facilitates lagging strand DNA replication in the Thermococcales.

Nucleic acids research·2026
Same author

The LARP1 RRM functions as a ribosome responsive regulator of TOP mRNAs.

bioRxiv : the preprint server for biology·2026
Same author

Rerouting reductant flux via protein tethering enhances biohydrogen production in Thermococcus kodakarensis.

Applied microbiology and biotechnology·2026
Same journal

Genetic Impacts on Variability of Body Fat Distribution Uncover Gene-Environment and Gene-Gene Interactions.

bioRxiv : the preprint server for biology·2026
Same journal

16S ribosomal RNA modification drives transcript-specific translation efficiency.

bioRxiv : the preprint server for biology·2026
Same journal

FlcE latches onto the FliL-stator complex to turbocharge flagellar motility in <i>Borrelia burgdorferi</i>.

bioRxiv : the preprint server for biology·2026
Same journal

Synaptic pruning, myelination and the emergence of psychiatric disorders in late adolescence.

bioRxiv : the preprint server for biology·2026
Same journal

Structural and functional insights into the Rcs phosphorelay.

bioRxiv : the preprint server for biology·2026
Same journal

The structural basis of RanGAP1 regulation and catalysis in nuclear transport.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jan 16, 2026

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

4.4K

A sequence-specific RNA acetylation catalyst.

Supuni Thalalla Gamage1, Shereen Howpay Manage1, Aldema Sas-Chen2

  • 1Chemical Biology Laboratory, National Cancer Institute, Frederick, MD, 21702, USA.

Biorxiv : the Preprint Server for Biology
|October 1, 2025
PubMed
Summary
This summary is machine-generated.

Researchers characterized Thermococcus kodakarensis Nat10 (TkNat10), an enzyme crucial for archaeal thermotolerance. TkNat10 acetylates RNA, a modification vital for organism fitness at high temperatures.

More Related Videos

Antibody-Free Assay for RNA Methyltransferase Activity Analysis
08:31

Antibody-Free Assay for RNA Methyltransferase Activity Analysis

Published on: July 9, 2019

7.6K
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

7.4K

Related Experiment Videos

Last Updated: Jan 16, 2026

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

4.4K
Antibody-Free Assay for RNA Methyltransferase Activity Analysis
08:31

Antibody-Free Assay for RNA Methyltransferase Activity Analysis

Published on: July 9, 2019

7.6K
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

7.4K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Archaea Research

Background:

  • N4-acetylcytidine (ac4C) is a widespread RNA modification.
  • Cytidine acetyltransferases catalyze ac4C incorporation.
  • Archaea possess unique mechanisms for thermotolerance.

Purpose of the Study:

  • Biochemically characterize Thermococcus kodakarensis Nat10 (TkNat10).
  • Investigate TkNat10's role in archaeal thermotolerance.
  • Define TkNat10's substrate specificity and cofactor requirements.

Main Methods:

  • Purification and biochemical assays of TkNat10.
  • RNA acetylation assays using diverse substrates.
  • Transcriptome-wide analysis of TkNat10 targets.
  • High-throughput mutagenesis for substrate recognition studies.

Main Results:

  • TkNat10 is essential for T. kodakarensis fitness at high temperatures.
  • TkNat10 exhibits robust, stand-alone activity dependent on temperature, ATP, and acetyl-CoA.
  • TkNat10 preferentially modifies unstructured RNAs with a 5'-CCG-3' sequence.
  • TkNat10 can be engineered to utilize non-native acyl-CoA donors.

Conclusions:

  • TkNat10's catalytic activity is critical for archaeal thermotolerance.
  • Established sequence and structural determinants for TkNat10 substrate recognition.
  • TkNat10 serves as a tool for studying ac4C modifications and RNA-protein interactions.