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

Mitochondrial preprotein translocase

N Pfanner1, E A Craig, A Hönlinger

  • 1Institut für Biochemie und Molekularbiologie, Universität Freiburg, Germany. pfanner@ruf.uni-freiburg.de

Annual Review of Cell and Developmental Biology
|January 1, 1997
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

Shaping the mitochondrial inner membrane in health and disease.

Journal of internal medicine·2020
Same author

The diverse roles of J-proteins, the obligate Hsp70 co-chaperone.

Reviews of physiology, biochemistry and pharmacology·2006
Same author

A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers.

Cellular and molecular life sciences : CMLS·2002
Same author

Hsp70 proteins in protein translocation.

Advances in protein chemistry·2002
Same author

Sorting of preproteins into mitochondria.

Chembiochem : a European journal of chemical biology·2002
Same author

Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.

Molecular biology of the cell·2001
Same journal

Hidden Messages in Extracellular Vesicles: Cross-Kingdom RNA Communication in Plant and Microbe Interactions.

Annual review of cell and developmental biology·2026
Same journal

mRNA-Scaffolded Cytoplasmic Compartments.

Annual review of cell and developmental biology·2026
Same journal

Developmental Programming of Human Kidney Function.

Annual review of cell and developmental biology·2026
Same journal

The Translation of Genetic Information in Neurodevelopment.

Annual review of cell and developmental biology·2026
Same journal

The Origin and Early Evolution of Fungi: Challenges, Inferences, and Principles.

Annual review of cell and developmental biology·2026
Same journal

Interstitial Spaces: A Basolateral Source of Structure and Signals.

Annual review of cell and developmental biology·2026
See all related articles

Mitochondria import proteins using dynamic membrane complexes. These translocases, involving receptors, pores, and motors, guide protein translocation via energy input and specific sequence recognition.

Area of Science:

  • Mitochondrial biology
  • Protein import mechanisms
  • Cellular and molecular biology

Background:

  • Mitochondria import the majority of their proteins from the cytosol.
  • Specialized protein complexes in the outer and inner mitochondrial membranes mediate this import process.
  • Understanding these mechanisms is crucial for cellular function and disease research.

Purpose of the Study:

  • To elucidate the molecular mechanisms of protein import into mitochondria.
  • To describe the components and dynamics of mitochondrial protein translocases.
  • To explain the role of signal sequences and energy sources in protein translocation.

Main Methods:

  • Analysis of mitochondrial outer and inner membrane protein translocase complexes.
  • Investigation of protein-protein interactions within translocases.

Related Experiment Videos

  • Examination of the role of signal sequences and membrane potential in protein import.

    • Main Results:

    • Mitochondrial protein import involves dynamic translocase complexes in both outer and inner membranes.
    • The outer membrane translocase includes import receptors and a general pore.
    • The inner membrane translocase features a channel and an Hsp70-based import motor, utilizing membrane potential and ATP.
    • The 'acid chain hypothesis' suggests acidic patches guide positively charged signal sequences.

    Conclusions:

    • Mitochondrial protein import is a highly regulated, multi-step process.
    • The dynamic nature of translocases allows for precise sorting of proteins.
    • Energy sources like inner membrane potential and ATP are essential for efficient import.