Related Experiment Video
Updated: Jun 15, 2026
08:58
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Co-evolution-driven switch of J-protein specificity towards an Hsp70 partner
Sebastian Pukszta1, Brenda Schilke, Rafal Dutkiewicz
1Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, Gdansk, Poland.
EMBO Reports
|March 13, 2010
Summary
Gene duplication and protein evolution are clarified. Changes in J-protein Jac1 structure accompanied specialization of the Hsp70 Ssq1 chaperone, linking partner protein evolution to functional divergence after gene duplication.
Area of Science:
- Molecular biology
- Biochemistry
- Evolutionary biology
Background:
- Understanding how protein-protein interactions evolve after gene duplication is crucial for deciphering molecular evolution.
- The yeast mitochondrial heat shock protein 70 (mtHsp70) and J-protein system serves as a model for studying chaperone-client interactions.
Purpose of the Study:
- To investigate the molecular mechanisms underlying the preservation or loss of protein-protein interactions following gene duplication.
- To determine if changes in partner proteins correlate with the specialization of duplicated genes, using the yeast mtHsp70:J-protein system.
Main Methods:
- Comparative analysis of Hsp70 and J-protein sequences across species.
- Functional characterization of J-protein variants with altered J-domain lengths.
- Investigating the interaction between specialized Hsp70 (Ssq1) and its J-protein partner (Jac1).
Main Results:
- The specialized Hsp70 Ssq1, arising from mtHsp70 duplication, correlates with structural and functional changes in its J-protein partner, Jac1.
- A shorter J-domain in Jac1 is conserved across species, suggesting a single deletion event.
- Engineering a longer J-domain in a short Jac1 variant restored its ability to partner with multifunctional Hsp70.
Conclusions:
- Demonstrates a causal link between alterations in a J-protein partner and the functional specialization of a duplicated Hsp70.
- Provides insights into the evolutionary mechanisms driving protein interaction divergence after gene duplication.
- Highlights the role of protein domain evolution in shaping specialized chaperone functions.
Related Concept Videos
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:14GTPases and their Regulation
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Large G-proteins, also known...
02:14GTPases and their Regulation
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Large G-proteins, also known...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...