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

Chaperones get Hip. Protein folding

T Ziegelhoffer1, J L Johnson, E A Craig

  • 1Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Current Biology : CB
|March 1, 1996
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

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

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

Molecular biology of the cell·2001
Same author

The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.

Molecular and cellular biology·2001
Same author

The role of Sis1 in the maintenance of the [RNQ+] prion.

The EMBO journal·2001
Same author

The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.

The Journal of biological chemistry·2001

Researchers discovered Hip, a new co-chaperone that interacts with Hsp70. This finding highlights the intricate nature of the Hsp70 chaperone machine, crucial for early protein folding processes within cells.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Biochemistry

Background:

  • Heat shock proteins (HSPs), particularly Hsp70, play critical roles in cellular protein homeostasis.
  • The Hsp70 chaperone machine is essential for various protein processing events, including folding, unfolding, and transport.
  • Understanding the regulatory mechanisms of Hsp70 is key to deciphering cellular protein folding pathways.

Purpose of the Study:

  • To identify and characterize novel factors that modulate Hsp70 activity.
  • To elucidate the molecular mechanisms underlying Hsp70-mediated protein folding.
  • To investigate the role of newly discovered co-chaperones in the Hsp70 chaperone machine.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions.

Related Experiment Videos

  • In vitro chaperone assays to measure Hsp70 activity.
  • Yeast three-hybrid screening for identifying interacting partners.

    • Main Results:

    • Identification of a novel co-chaperone, designated Hip.
    • Demonstration of direct interaction between Hip and Hsp70.
    • Evidence that Hip modulates the ATPase activity of Hsp70, influencing its chaperone function.

    Conclusions:

    • The discovery of Hip adds a new layer of complexity to the Hsp70 chaperone machine.
    • Hip's interaction with Hsp70 is crucial for regulating early steps of protein folding.
    • This finding opens new avenues for research into chaperone-assisted protein folding and cellular stress responses.