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

Spontaneous subunit exchange in porcine liver fructose-1,6-bisphosphatase.

S W Nelson1, R B Honzatko, H J Fromm

  • 1Department of Biochemistry, Biophysics, and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USA.

FEBS Letters
|March 21, 2001
PubMed
Summary

Mammalian fructose-1,6-bisphosphatase tetramers can exchange subunits, challenging previous assumptions. This subunit exchange is influenced by ligands and may impact enzyme regulation.

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

Efficacy of detergent-based cleaning and wiping against SARS-CoV-2 on high-touch surfaces.

Letters in applied microbiology·2023
Same author

Evaluation of surface disinfection methods to inactivate the beta coronavirus Murine Hepatitis Virus.

Journal of occupational and environmental hygiene·2022
Same author

Prevalence of Influenza A Virus in Exhibition Swine during Arrival at Agricultural Fairs.

Zoonoses and public health·2016
Same author

Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis.

Photochemistry and photobiology·2001
Same author

Subperiosteal and intraosseous connective tissue grafts for pocket reduction: a 9- to 13-year retrospective case series report.

Journal of periodontology·2001
Same author

Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure.

The Journal of biological chemistry·2001

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein dynamics

Background:

  • Mammalian fructose-1,6-bisphosphatase (FBPase) is a key metabolic enzyme.
  • Tetrameric structure of FBPase was previously thought to be stable, with no subunit exchange.

Purpose of the Study:

  • To investigate the potential for subunit exchange in mammalian FBPase tetramers.
  • To understand how ligands affect FBPase subunit dynamics and allosteric regulation.

Main Methods:

  • Engineering a mutant FBPase with altered electrostatic charge on its subunits.
  • Monitoring subunit exchange using non-denaturing gel electrophoresis and anion exchange chromatography.
  • Assessing the impact of active site ligands (fructose 6-phosphate) and allosteric regulators (AMP) on exchange.

Related Experiment Videos

Main Results:

  • Engineered FBPase with altered charge spontaneously exchanges subunits with wild-type enzyme.
  • Subunit exchange reaches equilibrium within 5 hours at 4°C.
  • Active site ligands inhibit monomer exchange but allow dimer exchange; AMP abolishes all exchange.

Conclusions:

  • Subunit exchange is a possible phenomenon in mammalian FBPase tetramers.
  • Ligand binding significantly modulates the extent and type of subunit exchange.
  • These exchange dynamics may be integral to the allosteric regulatory mechanism of FBPase.