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

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.7K
Mismatch Repair01:36

Mismatch Repair

43.5K
Overview
43.5K
Mismatch Repair01:20

Mismatch Repair

6.3K
Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
6.3K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K

You might also read

Related Articles

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

Sort by
Same author

Mechanistically Defined Epoxide- and Aziridine-2-carboxamide Electrophiles Enable Stereoselective Covalent RNA Modulation.

bioRxiv : the preprint server for biology·2026
Same author

Eight Triplex-Binding Molecules from Four Chemical Classes Broadly Recognize the MALAT1 Triple Helix.

Molecules (Basel, Switzerland)·2025
Same author

Understanding the Molecular Basis of Miller-Dieker Syndrome.

International journal of molecular sciences·2025
Same author

Exercise sensitizes the pressure diuresis response: shifting immune landscapes may underlie renal adaptations.

American journal of physiology. Renal physiology·2025
Same author

A tRNA gene potential to activate interferon signaling involves selective termination and is suppressible by La protein/SSB.

Nucleic acids research·2025
Same author

Multi-Omics Approach Reveals Genes and Pathways Affected in Miller-Dieker Syndrome.

Molecular neurobiology·2024

Related Experiment Video

Updated: Jan 16, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

3.9K

Mutational Analysis Reveals Functional Roles of METTL16 Domains and Residues.

Kurtis Breger1, Ian P Schowe1, Noah A Springer1

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.

Biology
|September 27, 2025
PubMed
Summary

Human methyltransferase-like protein 16 (METTL16) is crucial for RNA methylation. This study reveals specific residues and regions critical for U6 snRNA and S-adenosylmethionine (SAM) binding and methylation activity.

Keywords:
METTL16N6-methyladenosineU6 snRNAmethyltransferase

More Related Videos

Identification of Functionally-Relevant Lentivirus Integration Sites in an Insertional Mutagenesis Cell Library
07:28

Identification of Functionally-Relevant Lentivirus Integration Sites in an Insertional Mutagenesis Cell Library

Published on: January 10, 2025

700
Implementation of In Vitro Drug Resistance Assays: Maximizing the Potential for Uncovering Clinically Relevant Resistance Mechanisms
08:46

Implementation of In Vitro Drug Resistance Assays: Maximizing the Potential for Uncovering Clinically Relevant Resistance Mechanisms

Published on: December 9, 2015

11.1K

Related Experiment Videos

Last Updated: Jan 16, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

3.9K
Identification of Functionally-Relevant Lentivirus Integration Sites in an Insertional Mutagenesis Cell Library
07:28

Identification of Functionally-Relevant Lentivirus Integration Sites in an Insertional Mutagenesis Cell Library

Published on: January 10, 2025

700
Implementation of In Vitro Drug Resistance Assays: Maximizing the Potential for Uncovering Clinically Relevant Resistance Mechanisms
08:46

Implementation of In Vitro Drug Resistance Assays: Maximizing the Potential for Uncovering Clinically Relevant Resistance Mechanisms

Published on: December 9, 2015

11.1K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Human methyltransferase-like protein 16 (METTL16) methylates U6 small nuclear RNA (snRNA) and other RNAs.
  • Existing crystal structures of METTL16 lack detailed structure-function insights for specific residues.

Purpose of the Study:

  • To elucidate the functional roles of specific METTL16 domains and amino acid residues.
  • To understand the molecular mechanisms of U6 snRNA and S-adenosylmethionine (SAM) binding.
  • To investigate the impact of cancer-associated mutations on METTL16 activity.

Main Methods:

  • Site-directed mutagenesis to create 38 METTL16 mutants, including seven cancer-associated variants.
  • Electrophoretic mobility shift assays (EMSAs) to assess U6 snRNA binding.
  • Single-turnover kinetic assays to measure methylation rates and SAM binding.

Main Results:

  • The C-terminal vertebrate conserved regions (VCRs), especially the R382-R388 region, are key for cooperative U6 snRNA binding.
  • The METTL16 K-loop appears to block SAM binding, with mutants showing tighter SAM interaction.
  • Residues E133 and F227 stabilize SAM binding; mutations in the 184NPPF187 core or R282A abolish activity.
  • Cancer-associated mutants G110C and R241Dfs*2 exhibit reduced methylation activity.

Conclusions:

  • Specific domains and residues significantly influence METTL16's substrate binding and catalytic activity.
  • The VCRs and K-loop play distinct roles in RNA and cofactor binding.
  • This study provides critical structure-function insights into METTL16-mediated RNA methylation.