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Cochaperonins are histone-binding proteins

M A Bonardi1, E Giovanetti, G Legname

  • 1Department of Immunology, Italfarmaco Research Centre, Cinisello Balsamo, Italy.

Biochemical and Biophysical Research Communications
|January 5, 1995
PubMed
Summary
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Cochaperonins (cpn10) bind directly to histones, revealing a novel cellular function independent of chaperonins (cpn60). These findings identify histones as key cpn10 binding partners in eukaryotic cells.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Interactions

Background:

  • Cochaperonins (cpn10) are known to assist chaperonins (cpn60) in ATP-dependent protein folding.
  • Cpn10 can also be secreted and exhibit biological activities independently of cpn60.

Purpose of the Study:

  • To investigate potential cellular binding sites for cochaperonins (cpn10) that mediate their independent biological activities.
  • To identify proteins that interact with cpn10 in eukaryotic cells.

Main Methods:

  • Binding studies using iodinated cochaperonins (cpn10).
  • Analysis of whole cells and electrophoretically separated eukaryotic cell lysates.
  • Protein identification following cpn10 binding detection.

Main Results:

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  • No significant cpn10 binding was detected on whole cells.
  • Binding of cpn10 to proteins in eukaryotic cell lysates was observed.
  • The identified binding proteins were histones, including core histones (H2A, H2B, H3, H4) and linker histone H1.

Conclusions:

  • Cochaperonins (cpn10) are histone-binding proteins.
  • Histones represent a novel class of cellular partners for cpn10, mediating functions independent of the chaperonin (cpn60) system.