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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

You might also read

Related Articles

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

Sort by
Same author

A biosynthetic survey of hypocrealean biocontrol fungi.

Nature chemical biology·2026
Same author

Expanding the scope of redox-balance growth coupling techniques with a carbon cofeeding strategy.

bioRxiv : the preprint server for biology·2026
Same author

Leveraging a synthetic biology approach to enhance BCG-mediated expansion of Vγ9Vδ2 T cells.

PloS one·2026
Same author

Quantitative Dissection of Agrobacterium Virulence to Generate a Synthetic Ti Plasmid.

ACS synthetic biology·2026
Same author

Synthetic biology for heterologous expression and engineering of fungal polyketide synthases.

Natural product reports·2026
Same author

Enzymology and Structural Basis of Glycosyltransferases Involved in Saponin C28 Carboxylic Acid <i>O</i>‑d‑Fucosylation.

JACS Au·2025

Related Experiment Video

Updated: Jun 13, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.2K

Biosensor Guided Polyketide Synthases Engineering for Optimization of Domain Exchange Boundaries.

Elias Englund1,2, Matthias Schmidt1,3,4, Alberto A Nava1,5

  • 1Joint BioEnergy Institute, Emeryville, CA, USA.

Nature Communications
|August 12, 2023
PubMed
Summary

Researchers developed a biosensor to create new hybrid polyketide synthases (PKSs). This method identifies stable engineered PKS variants, enabling the production of novel molecules with improved structural integrity.

More Related Videos

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes T&#252;6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

17.2K
A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
07:59

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

Published on: October 4, 2019

9.9K

Related Experiment Videos

Last Updated: Jun 13, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.2K
From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes T&#252;6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

17.2K
A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
07:59

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products

Published on: October 4, 2019

9.9K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Type I modular polyketide synthases (PKSs) are complex enzymes crucial for natural product biosynthesis.
  • Engineering PKSs to create novel molecules is challenging due to instability and misfolding of modified enzymes.

Purpose of the Study:

  • To develop a high-throughput method for identifying stable, engineered PKS variants.
  • To optimize domain boundaries in hybrid PKSs to maintain structural integrity and activity.

Main Methods:

  • Development of a fluorescence-based solubility biosensor for rapid screening of PKS variants.
  • Engineering of acyltransferase (AT)-exchanged PKS hybrids with varied domain boundaries.
  • Systematic probing of AT linker regions to identify optimal domain insertion sites.

Main Results:

  • Identification of engineered PKS variants with wild-type production levels using the biosensor.
  • Determination of specific domain boundary positions that enhance PKS structural integrity.
  • Successful creation of stable, hybrid PKSs capable of producing novel molecules.

Conclusions:

  • The developed biosensor provides an efficient tool for engineering complex enzymes like PKSs.
  • Optimized domain boundaries are critical for the stability and functionality of hybrid PKSs.
  • This work facilitates the production of novel compounds through synthetic biology approaches.