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

22.9K
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...
22.9K
tRNA Activation02:26

tRNA Activation

8.6K
8.6K
Histone Modification02:32

Histone Modification

16.1K
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...
16.1K
Histone Modification02:32

Histone Modification

4.5K
4.5K
From DNA to Protein03:06

From DNA to Protein

22.3K
The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
22.3K
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

You might also read

Related Articles

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

Sort by
Same author

Functional divergence and conservation in the QueC protein family (PF06508): from tRNA modification to anti-phage defense.

The Biochemical journal·2026
Same author

Engineering Biosensors to Enhance Monoterpene Indole Alkaloid Production in Yeast.

bioRxiv : the preprint server for biology·2026
Same author

IL-9 orchestrates MDSC expansion and inflammatory programming to amplify immunopathology during experimental cerebral malaria.

Microbial pathogenesis·2026
Same author

The <i>Escherichia coli</i> Radical SAM Enzyme YhcC Substitutes for the FAD-Dependent Oxidase Activity of MnmC in 5-Methylaminomethyl-2-Thiouridine tRNA Modification Under Anaerobic Conditions.

bioRxiv : the preprint server for biology·2026
Same author

Retention modeling of oligonucleotides on an amide-based HILIC column: A descriptor-driven approach.

Journal of chromatography. A·2026
Same author

Functional Divergence and Conservation in the QueC Protein Family (PF06508): From tRNA Modification to Anti-Phage Defense.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jan 29, 2026

Profiling of H3K4me3 Modification in Plants using Cleavage under Targets and Tagmentation
09:48

Profiling of H3K4me3 Modification in Plants using Cleavage under Targets and Tagmentation

Published on: April 22, 2022

4.5K

tRNA Modification Profiles and Codon-Decoding Strategies in Methanocaldococcus jannaschii.

Ningxi Yu1, Manasses Jora1, Beulah Solivio1

  • 1Rieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.

Journal of Bacteriology
|February 13, 2019
PubMed
Summary

Researchers mapped tRNA modifications in Methanocaldococcus jannaschii, discovering a new modification and revealing archaeal decoding strategies similar to bacteria. This work enhances understanding of archaeal tRNA modification patterns.

Keywords:
5-cyanomethyl-2-thiouridineLC-MS/MSanticodon looparchaeamodified nucleosidesposttranscriptional modificationtRNA

More Related Videos

Metabolic Labeling and Profiling of Transfer RNAs Using Macroarrays
10:56

Metabolic Labeling and Profiling of Transfer RNAs Using Macroarrays

Published on: January 16, 2018

6.1K
Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
10:41

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

Published on: June 24, 2019

8.8K

Related Experiment Videos

Last Updated: Jan 29, 2026

Profiling of H3K4me3 Modification in Plants using Cleavage under Targets and Tagmentation
09:48

Profiling of H3K4me3 Modification in Plants using Cleavage under Targets and Tagmentation

Published on: April 22, 2022

4.5K
Metabolic Labeling and Profiling of Transfer RNAs Using Macroarrays
10:56

Metabolic Labeling and Profiling of Transfer RNAs Using Macroarrays

Published on: January 16, 2018

6.1K
Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
10:41

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

Published on: June 24, 2019

8.8K

Area of Science:

  • Molecular Biology
  • Genomics
  • Biochemistry

Background:

  • Transfer RNAs (tRNAs) are crucial for decoding messenger RNA (mRNA), with posttranscriptional modifications enhancing efficiency and accuracy.
  • While tRNA modifications are well-studied in bacteria and eukaryotes, archaeal tRNA modification patterns and their role in codon-decoding remain less understood.
  • Haloferax volcanii is the only archaeon with extensively localized tRNA modifications; broader characterization is needed for other archaeal species.

Purpose of the Study:

  • To characterize and map posttranscriptional modifications on 34 unique tRNA sequences of Methanocaldococcus jannaschii.
  • To gain insights into archaeal tRNA modification patterns and codon-decoding strategies.
  • To compare archaeal tRNA modification profiles with those of bacteria and eukaryotes.

Main Methods:

  • Liquid chromatography and tandem mass spectrometry were employed to identify and localize tRNA modifications.
  • RNA modification mapping was performed on 34 unique tRNA sequences from Methanocaldococcus jannaschii.
  • Comparative analysis was conducted with tRNA modification profiles from Haloferax volcanii, bacteria, and eukaryotes.

Main Results:

  • A novel modified nucleoside, 5-cyanomethyl-2-thiouridine (cnm5s2U), was discovered and mapped to position 34 of M. jannaschii tRNAs.
  • Wysosine pathway modifications were detected beyond the canonical tRNA Phe, a pattern observed in eukaryotes.
  • Modification profiles of M. jannaschii tRNA anticodon loops were characterized, revealing similarities to bacterial decoding strategies, with potentially greater modification at position 37 compared to H. volcanii.

Conclusions:

  • Methanocaldococcus jannaschii exhibits unique archaeal tRNA modifications alongside conserved ones found in bacteria and eukaryotes.
  • The study provides high-quality mapping of tRNA anticodon loops, significantly advancing the understanding of archaeal tRNA modification profiles.
  • M. jannaschii employs codon-decoding strategies similar to bacteria, with extensive modifications at position 37 suggesting a specialized role in decoding.