Physicochemical Properties of the Mammalian Molecular Chaperone HSP60
| Autor: | Toshihiko Oka, Akira Kitamura, Michiro Otaka, Tomoya Okamoto, Masasuke Yoshida, Ewa Grave, Masataka Kinjo, Masako Tanabe, Hiroshi Kubota, Hiroki Takahashi, Ryuichi Ishida, Fumihiro Motojima, Hideaki Itoh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chaperonin animal structures Chemical Phenomena Catalysis Article GroEL Chaperonin lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound Adenosine Triphosphate Heat shock protein Chaperonin 10 Animals Humans Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Spectroscopy 030102 biochemistry & molecular biology Molecular Structure Chemistry Organic Chemistry fungi molecular chaperone HSP60 General Medicine GroES Chaperonin 60 Computer Science Applications Adenosine diphosphate 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 Multiprotein Complexes Biophysics Protein folding Adenosine triphosphate Molecular Chaperones Protein Binding |
| Zdroj: | International Journal of Molecular Sciences; Volume 19; Issue 2; Pages: 489 International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 19, Iss 2, p 489 (2018) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms19020489 |
| Popis: | The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmetric complex, and GroEL exists as double rings regardless of the presence of adenosine triphosphate (ATP). Its mammalian chaperonin homolog, heat shock protein, HSP60, and co-chaperonin, HSP10, play an essential role in protein folding by capturing unfolded proteins in the HSP60/HSP10 complex. However, the structural transition in ATPase-dependent reaction cycle has remained unclear. We found nucleotide-dependent association and dissociation of the HSP60/HSP10 complex using various analytical techniques under near physiological conditions. Our results showed that HSP60 exist as a significant number of double-ring complexes (football- and bullet-type complexes) and a small number of single-ring complexes in the presence of ATP and HSP10. HSP10 binds to HSP60 in the presence of ATP, which increased the HSP60 double-ring formation. After ATP is hydrolyzed to Adenosine diphosphate (ADP), HSP60 released the HSP10 and the dissociation of the double-ring to single-rings occurred. These results indicated that HSP60/HSP10 undergoes an ATP-dependent transition between the single- and double-rings in their system that is highly distinctive from the GroEL/GroES system particularly in the manner of complex formation and the roles of ATP binding and hydrolysis in the reaction cycle. |
| Databáze: | OpenAIRE |
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