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Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes
Affiliation:1. Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada;2. Department of Chemistry and Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada;3. Medical Proteomics Unit, Office for Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand;4. Center of Biological and Health Sciences, Federal University of São Carlos, São Carlos, SP 13560-970, Brazil;5. Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK;6. Department of Biochemistry and Biophysics, Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94158, USA;7. São Carlos Institute of Chemistry, University of São Paulo, São Carlos, SP 13566-590, Brazil;8. Institute of Physics, University of São Paulo, São Paulo, SP 05508-090, Brazil;9. Institute of Chemistry, University of Campinas (UNICAMP), Campinas, SP 13083-970, Brazil;10. Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, Canada;11. Brazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, SP 13083-100, Brazil
Abstract:
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  • Keywords:AAA+ proteins  molecular chaperones  R2TP  PAQosome  macromolecular complex assembly  protein folding  ATPases  RUVBL1/2
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