Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.

Autor:	Sadat A; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Tiwari S; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Sunidhi S; Department of Computational Biology, Indraprastha Institute of Information Technology-Delhi, New Delhi 110020, India., Chaphalkar A; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Kochar M; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Ali M; Department of Life Sciences, School of Natural Sciences, Shiv Nadar University, Greater Noida 201314, India., Zaidi Z; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Sharma A; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Verma K; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Narayana Rao KB; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Tripathi M; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Ghosh A; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Gautam D; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India., Atul; Department of Computational Biology, Indraprastha Institute of Information Technology-Delhi, New Delhi 110020, India., Ray A; Department of Computational Biology, Indraprastha Institute of Information Technology-Delhi, New Delhi 110020, India., Mapa K; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Department of Life Sciences, School of Natural Sciences, Shiv Nadar University, Greater Noida 201314, India., Chakraborty K; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Chemical and System Biology Unit, CSIR-Institute of Genomics and Integrative Biology, New Delhi 110025, India.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 May 03; Vol. 119 (18), pp. e2118465119. Date of Electronic Publication: 2022 Apr 29.
DOI:	10.1073/pnas.2118465119
Abstrakt:	The GroEL/ES chaperonin cavity surface charge properties, especially the negative charges, play an important role in its capacity to assist intracavity protein folding. Remarkably, the larger fraction of GroEL/ES negative charges are not conserved among different bacterial species, resulting in a large variation in negative-charge density in the GroEL/ES cavity across prokaryotes. Intriguingly, eukaryotic GroEL/ES homologs have the lowest negative-charge density in the chaperonin cavity. This prompted us to investigate if GroEL’s chaperoning mechanism changed during evolution. Using a model in vivo GroEL/ES substrate, we show that the ability of GroEL/ES to buffer entropic traps in the folding pathway of its substrate was partially dependent upon the negative-charge density inside its cavity. While this activity of GroEL/ES was found to be essential for Escherichia coli, it has been perfected in some organisms and diminished in others. However, irrespective of their charges, all the tested homologs retained their ability to regulate polypeptide chain collapse and remove enthalpic traps from folding pathways. The ability of these GroEL/ES homologs to buffer mutational variations in a model substrate correlated with their negative-charge density. Thus, Hsp60/10 chaperonins in different organisms may have changed to accommodate a different spectrum of mutations on their substrates.
Databáze:	MEDLINE
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