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Updated: May 29, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
Published on: December 29, 2021
Sugarcane Hsp101 is a hexameric chaperone that binds nucleotides.
Thiago C Cagliari1, Viviane C H da Silva, Júlio C Borges
1Institute of Chemistry, University of Campinas-UNICAMP, PO Box 6154, 13083-970, Campinas, SP, Brazil.
Researchers cloned and purified sugarcane Hsp101 (SHsp101), a protein involved in protein disaggregation. SHsp101 exhibits structural and functional traits common to the Clp/Hsp100 AAA+ chaperone family.
Area of Science:
- Biochemistry
- Molecular Biology
- Plant Science
Background:
- The Clp/Hsp100 AAA+ chaperone family aids in protein aggregate recovery.
- ClpB (E. coli) and Hsp104 (S. cerevisiae) are well-studied members, but knowledge of other orthologs, like plant Hsp101, is limited.
- Plant Hsp101 serves as a model to understand Hsp100 structure-function relationships and disaggregation roles.
Purpose of the Study:
- To clone and purify a sugarcane ortholog of Hsp100, named SHsp101.
- To characterize SHsp101's structural and functional properties.
- To investigate SHsp101's role within the Clp/Hsp100 AAA+ chaperone family.
Main Methods:
- Cloning of the sugarcane Hsp101 gene.
- Protein expression and purification of SHsp101.
- Biochemical assays to assess nucleotide binding and oligomeric state.
Main Results:
- SHsp101 was successfully cloned and purified from sugarcane cells.
- The purified SHsp101 exists as a folded hexamer.
- SHsp101 demonstrates nucleotide-binding capabilities.
Conclusions:
- SHsp101 possesses the characteristic structural and functional attributes of the Clp/Hsp100 AAA+ chaperone family.
- This study provides a foundation for further research into the specific functions of plant Hsp100 proteins in protein disaggregation.
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