Related Experiment Video

Updated: Jun 16, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins--identification of

Ohad Iosefson1, Abdussalam Azem

  • 1Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.

FEBS Letters
|February 16, 2010
PubMed

Insights

Mammalian heat-shock protein (mortalin) binds the tumor suppressor p53. This interaction enhances p53 DNA binding and reveals a new mortalin binding site on p53.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Interactions

Background:

  • Mammalian mitochondrial 70 kDa heat-shock protein (mortalin) is also found in the cytosol.
  • Cytosolic mortalin binds p53, inhibiting its nuclear translocation.
  • This interaction is critical for tumor suppressor regulation.

Purpose of the Study:

  • To develop a novel binding assay for studying p53-mortalin interactions.
  • To characterize the molecular details of the binding between p53 and mortalin.

Main Methods:

  • Development of a novel binding assay using purified proteins.
  • Analysis of protein-protein interactions between p53 and mortalin.

Main Results:

  • p53 binds to the peptide-binding site of mortalin.
  • This binding enhances the DNA-binding capacity of p53.
  • A previously unidentified mortalin binding site was discovered within the C-terminal domain of p53.

Conclusions:

  • The study elucidates specific binding sites and functional consequences of the p53-mortalin interaction.
  • Findings provide new insights into the regulation of p53 by mortalin.
  • The developed assay is valuable for further research on mortalin's role in cellular processes.

More Related Videos

Reconstitution of Msp1 Extraction Activity with Fully Purified Components05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

An Improved Method to Isolate Mitochondrial Contact Sites07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

Related Concept Videos

Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...