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 Concept Videos

Mismatch Repair01:36

Mismatch Repair

Overview
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...

You might also read

Related Articles

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

Sort by
Same author

J-domain proteins: from molecular mechanisms to diseases.

Cell stress & chaperones·2025
Same author

The Use of Small Molecules to Correct Defects in CFTR Folding, Maturation, and Channel Activity.

Current chemical biology·2025
Same author

Type I Hsp40s/DnaJs aggregates exhibit features reminiscent of amyloidogenic structures.

The FEBS journal·2024
Same author

Novel functions of the ER-located Hsp40s DNAJB12 and DNAJB14 on proteins at the outer mitochondrial membrane under stress mediated by CCCP.

Molecular and cellular biochemistry·2023
Same author

DNAJB12 and Hsp70 Mediate Triage of Misfolded Membrane Proteins for Proteasomal versus Lysosomal Degradation.

Autophagy reports·2023
Same author

Specification of Hsp70 Function by Hsp40 Co-chaperones.

Sub-cellular biochemistry·2022
Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
See all related articles

Related Experiment Video

Updated: May 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Swapping nucleotides, tuning Hsp70.

Douglas M Cyr1

  • 1Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. dmcyr@med.unc.edu

Cell
|June 17, 2008
PubMed
Summary
This summary is machine-generated.

New crystal structures reveal how heat shock protein 70 (Hsp70) interacts with its nucleotide exchange factor (NEF) Hsp110. These findings clarify how NEF action directs Hsp70

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Tuning Degradation to Achieve Specific and Efficient Protein Depletion
05:11

Tuning Degradation to Achieve Specific and Efficient Protein Depletion

Published on: July 20, 2019

Related Experiment Videos

Last Updated: May 7, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Tuning Degradation to Achieve Specific and Efficient Protein Depletion
05:11

Tuning Degradation to Achieve Specific and Efficient Protein Depletion

Published on: July 20, 2019

Area of Science:

  • Molecular biology
  • Protein biochemistry
  • Structural biology

Background:

  • Molecular chaperones, including heat shock protein 70 (Hsp70), are essential for proper protein folding and cellular function.
  • Heat shock protein 110 (Hsp110) acts as a nucleotide exchange factor (NEF) for Hsp70, modulating its activity.
  • Understanding the interaction between Hsp70 and NEFs is critical for deciphering chaperone-mediated protein homeostasis.

Purpose of the Study:

  • To elucidate the structural basis of Hsp70-Hsp110 interaction.
  • To provide mechanistic insights into how NEF activity specifies Hsp70 cellular functions.
  • To offer a detailed view of the Hsp70-NEF complex at the atomic level.

Main Methods:

  • X-ray crystallography was employed to determine the three-dimensional structures of Hsp70 in complex with Hsp110.
  • Comparative structural analysis of the Hsp70-Hsp110 complexes.

Main Results:

  • Crystal structures of Hsp70 complexed with Hsp110 were determined.
  • These structures reveal the precise atomic interactions between Hsp70 and its NEF, Hsp110.
  • The structural data provide a foundation for understanding the mechanism of NEF-mediated Hsp70 regulation.

Conclusions:

  • The crystal structures offer unprecedented insights into the Hsp70-Hsp110 chaperone machinery.
  • These findings advance our comprehension of how NEF action dictates Hsp70's role in cellular processes.
  • The study provides a structural framework for future investigations into chaperone function and dysfunction.