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

Sequential action of two hsp70 complexes during protein import into mitochondria

M Horst1, W Oppliger, S Rospert

  • 1Biozentrum, Universität Basel, Switzerland.

The EMBO Journal
|April 15, 1997
PubMed
Summary

Mitochondrial chaperone mhsp70 utilizes distinct complexes for protein transport and folding within mitochondria. These complexes, import and folding, facilitate precursor protein processing.

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

Long-Range Transverse-Momentum Correlations and Radial Flow in Pb-Pb Collisions at the LHC.

Physical review letters·2026
Same author

Search for Quasiparticle Scattering in the Quark-Gluon Plasma with Jet Splittings in pp and Pb-Pb Collisions at sqrt[s_{NN}]=5.02  TeV.

Physical review letters·2025
Same author

First Measurement of A=4 Hypernuclei and Antihypernuclei at the LHC.

Physical review letters·2025
Same author

Long-term follow-up after ureteral reimplantation in children: a 12-year analysis.

Pediatric surgery international·2025
Same author

Probing Strangeness Hadronization with Event-by-Event Production of Multistrange Hadrons.

Physical review letters·2025
Same author

Measurements of Chemical Potentials in Pb-Pb Collisions at sqrt[s_{NN}]=5.02  TeV.

Physical review letters·2024

Area of Science:

  • Mitochondrial biology
  • Protein homeostasis
  • Molecular chaperones

Background:

  • Mitochondrial chaperones are essential for protein folding and transport.
  • Mitochondrial heat shock protein 70 (mhsp70) plays a critical role in mitochondrial protein import and folding.

Purpose of the Study:

  • To elucidate the distinct functional complexes of mhsp70 involved in mitochondrial protein processing.
  • To understand how mhsp70 coordinates protein transport and folding within the mitochondrion.

Main Methods:

  • Investigating the composition and function of mhsp70 complexes.
  • Analyzing the role of different mhsp70 conformations (ADP and ATP) in complex formation.

Main Results:

  • Two distinct mhsp70 complexes were identified: an 'import complex' on the inner membrane and a 'folding complex' in the matrix.

Related Experiment Videos

  • The import complex comprises mhsp70, Tim44, and mGrpE, facilitating protein entry.
  • The folding complex consists of mhsp70, Mdj1, and mGrpE, promoting protein folding in the matrix.

    • Conclusions:

    • Mitochondrial chaperone mhsp70 operates through distinct protein complexes to mediate both protein import and folding.
    • The ADP-bound state of mhsp70 favors the import complex, while the ATP-bound state favors the folding complex.
    • This dual-complex mechanism allows a single chaperone to manage sequential steps in protein maturation within the same organelle.