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

Inducible Operons: lac Operon01:25

Inducible Operons: lac Operon

3.1K
The lac operon in Escherichia coli is a model for understanding inducible gene regulation and metabolic flexibility. It integrates local control by lactose and global regulation through catabolite repression, enabling E. coli to preferentially metabolize glucose when available and switch to lactose utilization when glucose is scarce.Structure and Function of the lac OperonThe lac operon contains three structural genes: lacZ (β-galactosidase), lacY (lactose permease), and lacA...
3.1K
Operons02:09

Operons

44.0K
Prokaryotes can control gene expression through operons—DNA sequences consisting of regulatory elements and clustered, functionally related protein-coding genes. Operons use a single promoter sequence to initiate transcription of a gene cluster (i.e., a group of structural genes) into a single mRNA molecule. The terminator sequence ends transcription. An operator sequence, located between the promoter and structural genes, prohibits the operon’s transcriptional activity if bound by...
44.0K
Operons02:09

Operons

14.2K
14.2K
Operon Model01:23

Operon Model

2.5K
The operon model represents a fundamental mechanism of gene regulation in prokaryotes, enabling coordinated expression of genes involved in related metabolic or functional pathways. Operons consist of structural genes, a promoter, and an operator, with transcription regulated by repressors, activators, and small effector molecules.Structure and Function of OperonsAn operon is a cluster of structural genes transcribed together under the control of a single promoter. The promoter region...
2.5K
Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

2.7K
The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
2.7K
Prokaryotic Transcriptional Activators and Repressors01:58

Prokaryotic Transcriptional Activators and Repressors

20.0K
The organization of prokaryotic genes in their genome is notably different from that of eukaryotes. Prokaryotic genes are organized, such that the genes for proteins involved in the same biochemical process or function are located together in groups. This group of genes, along with their regulatory elements, are collectively known as an operon. The functional genes in an operon are transcribed together to give a single strand of mRNA known as polycistronic mRNA.
Transcription of prokaryotic...
20.0K

You might also read

Related Articles

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

Sort by
Same author

GTP hydrolysis-powered zinc metallochaperones as molecular switches.

Current opinion in chemical biology·2026
Same author

Analysis of end-stage renal disease mediated by cuproptosis-related genes.

Clinical nephrology·2026
Same author

Mutations in RNA polymerase that drive the emergence of antibiotic resistance.

Current opinion in microbiology·2026
Same author

MeeY and YybP, two proteins regulated by manganese-sensing riboswitches, are required for Bacillus subtilis biofilm formation.

NPJ biofilms and microbiomes·2026
Same author

Pathways of copper import and utilization that support respiration in <i>Bacillus subtilis</i>.

mBio·2026
Same author

Self-activation by a C-terminal domain arginine finger regulates GTP hydrolysis in bacterial zinc metallochaperones.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Apr 29, 2026

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast
07:31

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast

Published on: June 30, 2022

1.9K

Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR).

Feng-Ming James Chang1, H Jerome Coyne1, Ciro Cubillas2

  • 1From the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102.

The Journal of Biological Chemistry
|May 17, 2014
PubMed
Summary

Copper-sensing operon repressor (CsoR) proteins prevent copper toxicity. Cu(I) binding to CsoR causes structural changes, including N-terminal tail folding, to derepress copper resistance genes.

Keywords:
CopperMetal Sensor ProteinMetalloregulationPhylogeneticsTranscription RepressorX-ray CrystallographyX-ray Scattering

More Related Videos

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.3K
Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

8.3K

Related Experiment Videos

Last Updated: Apr 29, 2026

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast
07:31

ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast

Published on: June 30, 2022

1.9K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

9.3K
Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

8.3K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Copper-sensing operon repressor (CsoR) is a key bacterial metalloregulatory protein family.
  • CsoR prevents cytoplasmic copper toxicity by regulating copper resistance genes.
  • The mechanism of Cu(I) binding to tetrameric CsoRs and subsequent transcriptional derepression is not fully understood.

Purpose of the Study:

  • To investigate the structural and dynamic changes in Geobacillus thermodenitrificans (Gt) CsoR upon copper(I) binding.
  • To understand the allosteric mechanism of Cu(I) sensing by CsoR proteins.
  • To establish the phylogenetic relationship of Gt CsoR to other CsoR/RcnR repressors.

Main Methods:

  • Phylogenetic analysis of 227 DUF156 protein members.
  • X-ray crystallography of Cu(I)-bound Gt CsoR at 2.56 Å resolution.
  • Nuclear Magnetic Resonance (NMR) spectroscopy of Gt CsoR.
  • Small-angle X-ray scattering (SAXS) experiments on N-terminally truncated Gt CsoR.

Main Results:

  • Phylogenetic analysis identified Gt CsoR as representative of pathogenic bacilli CsoRs.
  • Cu(I) binding induces an α2-helix kink and folds the flexible N-terminal tail over the copper-binding site.
  • NMR studies showed quenched dynamics of the N-terminal tail upon Cu(I) binding.
  • SAXS experiments revealed a more compact tetrameric structure upon Cu(I) binding.

Conclusions:

  • Cu(I) binding to Gt CsoR triggers significant structural rearrangements, including N-terminal tail modulation.
  • These changes likely mediate the allosteric derepression of copper resistance genes.
  • The findings provide insights into the conserved copper-sensing mechanism of CsoR/RcnR repressors.