Open AccessConserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes
Author(s) -
Anwar Sadat,
Satyam Tiwari,
S. Sunidhi,
Aseem Chaphalkar,
Manisha Kochar,
Md Khadem Ali,
Zainab Zaidi,
Akanksha Sharma,
Kanika Verma,
Kannan Boosi Narayana Rao,
Manjul Tripathi,
Asmita Ghosh,
Deepika Gautam,
Atul Atul,
Ray A,
Koyeli Mapa,
Kausik Chakraborty
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2118465119
Subject(s) - groel , chaperonin , protein folding , groes , biophysics , folding (dsp implementation) , escherichia coli , hsp60 , biology , substrate (aquarium) , chemistry , biochemistry , heat shock protein , gene , hsp70 , ecology , electrical engineering , engineering
Significance Hsp60/10 chaperonins are critical for cellular proteostasis in all kingdoms of life. In this study, we present that Hsp60/10 across different species have differences in the cavity properties and correlatively in their capability to remove entropic traps in folding pathways of GroEL/ES substrates; this is affected majorly by differences in the negative-charge density inside the chaperonin cavity. This dissimilarity leads to a remarkable difference between Hsp60/10 homologs in buffering mutational variations. However, most of them can remove nonnative contacts during folding of their substrates and alter the way the polypeptide chain undergoes hydrophobic collapse. We show that these homologs may have evolved specific modes of folding assistance by modulating cavity properties according to the requirements of their substrates.