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

From DNA to Protein03:06

From DNA to Protein

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...
The Central Dogma01:25

The Central Dogma

Overview
The Central Dogma01:20

The Central Dogma

The central dogma explains the flow of genetic information from DNA nucleotides to the amino acid sequence of proteins.
RNA is the Missing Link Between DNA and Proteins
In the early 1900s, scientists discovered that DNA stores all the information needed for cellular functions and that proteins perform most of these functions. However, the mechanisms of converting genetic information into functional proteins remained unknown for many years. Initially, it was believed that a single gene is...
Reporter Genes02:11

Reporter Genes

Reporter genes are a type of protein-coding gene that are often tagged to a gene of interest. Once inside a target cell, reporter genes usually produce visually identifiable characteristics like fluorescence and luminescence when expressed along with the gene of interest. Thus, reporter genes “report” the presence or absence of genes of interest in an organism, determine the gene expression pattern, or track the physical location of a DNA segment or protein in the cell.
Commonly used reporter...

You might also read

Related Articles

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

Sort by
Same author

Continuous Hypermutation and Evolution of Noncanonical Amino Acid Synthases.

ACS synthetic biology·2026
Same author

Discovery of Novel <i>N</i>-Linked Camptothecin Linker-Payloads to Access Antibody-Drug Conjugates with High Target-Mediated In Vivo Efficacy.

Journal of medicinal chemistry·2026
Same author

Design of Novel Exatecan-Amide Linker-Payloads for the Development of Stable, Low-Aggregating, and Highly Efficacious Antibody-Drug Conjugates.

Journal of medicinal chemistry·2026
Same author

Continuous hypermutation and evolution of noncanonical amino acid synthases.

bioRxiv : the preprint server for biology·2026
Same author

BoltzGen: Toward Universal Binder Design.

bioRxiv : the preprint server for biology·2025
Same author

Continuous Hypermutation and Evolution of Luciferase Variants.

ACS chemical biology·2025

Related Experiment Video

Updated: Jun 17, 2026

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion
13:11

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion

Published on: February 10, 2023

Efficient expression of tyrosine-sulfated proteins in E. coli using an expanded genetic code.

Chang C Liu1, Susan E Cellitti, Bernhard H Geierstanger

  • 1Department of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA.

Nature Protocols
|December 17, 2009
PubMed
Summary

Researchers developed a novel method for site-specific tyrosine sulfation in E. coli using an expanded genetic code. This technique allows efficient production of sulfated proteins, simplifying complex biological research.

More Related Videos

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

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Related Experiment Videos

Last Updated: Jun 17, 2026

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion
13:11

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion

Published on: February 10, 2023

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

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Synthetic Biology

Background:

  • Tyrosine sulfation is a crucial post-translational modification in eukaryotes, regulating vital cellular processes like communication and adhesion.
  • Existing methods for producing tyrosine-sulfated proteins are often complex and less versatile.

Purpose of the Study:

  • To establish a streamlined protocol for heterologous expression of selectively tyrosine-sulfated proteins in Escherichia coli.
  • To enable site-specific incorporation of sulfotyrosine using an expanded genetic code.

Main Methods:

  • Utilized an expanded genetic code in E. coli for co-translational insertion of sulfotyrosine in response to the amber nonsense codon (TAG).
  • Employed a plasmid (pSUPAR6-L3-3SY) encoding an orthogonal aminoacyl-tRNA synthetase specific for sulfotyrosine and its cognate tRNA.
  • Mutated the gene of interest to include TAG codons at desired sulfation sites and co-transformed with the expression plasmid.

Main Results:

  • Achieved efficient and high-fidelity overexpression of site-specifically tyrosine-sulfated proteins in E. coli.
  • Demonstrated a simpler and more versatile approach compared to in vitro enzymatic sulfation, chemical sulfation, and peptide synthesis.
  • The protocol allows protein production in under one week after cloning.

Conclusions:

  • The developed protocol offers a significantly simpler and more versatile method for producing site-specifically tyrosine-sulfated proteins.
  • This advancement facilitates research in areas requiring specific sulfation patterns, such as cell-cell communication and viral interactions.