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 Experiment Videos

Two-component and phosphorelay signal transduction.

J A Hoch1

  • 1Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. hoch@scripps.edu

Current Opinion in Microbiology
|April 4, 2000
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Aspartyl phosphates in the regulatory control of bacterial response.

Amino acids·2013
Same author

Developing inhibitors to selectively target two-component and phosphorelay signal transduction systems of pathogenic microorganisms.

Current medicinal chemistry·2004
Same author

Histidine kinase-mediated signal transduction systems of pathogenic microorganisms as targets for therapeutic intervention.

Current drug targets. Infectious disorders·2002
Same author

PAS-A domain of phosphorelay sensor kinase A: a catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis.

Proceedings of the National Academy of Sciences of the United States of America·2001
Same author

Functional Genomics of Gram-Positive Microorganisms: review of the meeting, San Diego, California, 24 to 28 June 2001.

Journal of bacteriology·2001
Same author

Keeping signals straight in phosphorelay signal transduction.

Journal of bacteriology·2001
Same journal

S-layers as natural building blocks for nanobiotechnology and synthetic biology.

Current opinion in microbiology·2026
Same journal

The role of the antimicrobial peptide nisin as a clean label food preservative.

Current opinion in microbiology·2026
Same journal

From coarse-grained metabolic rules to fine-grained control of microbial communities.

Current opinion in microbiology·2026
Same journal

Progress in engineered bacterial cancer therapies.

Current opinion in microbiology·2026
Same journal

Constraints on adaptive loss-of-function mutations during microbial metabolic interactions.

Current opinion in microbiology·2026
Same journal

Discovery of novel antimicrobials within microbiomes.

Current opinion in microbiology·2026
See all related articles

Bacteria use two-component and phosphorelay signal transduction systems to sense environmental changes. Understanding these systems

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Two-component and phosphorelay signal transduction systems are crucial for bacterial environmental sensing.
  • These systems regulate essential cellular processes like cell-cycle progression, pathogenicity, and development.

Purpose of the Study:

  • To elucidate the structures of interacting domains within these signal transduction systems.
  • To understand the molecular mechanisms underlying signal recognition and phosphotransfer.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography, NMR spectroscopy) were employed.
  • Biochemical assays were used to study protein-protein interactions and phosphotransfer activity.

Main Results:

Related Experiment Videos

  • Detailed structures of key interacting domains have been determined.
  • Mechanisms of specific molecular recognition between system components were revealed.
  • Insights into the phosphotransfer process at a molecular level were gained.

Conclusions:

  • Structural insights are critical for understanding bacterial signal transduction.
  • This knowledge facilitates the development of novel strategies targeting bacterial pathways.