Distinct metabolic states of a cell guide alternate fates of mutational buffering through altered proteostasis

Kanika Verma, Kanika Saxena, Rajashekar Donaka, Aseem Chaphalkar, Manish Kumar Rai, Anurag Shukla, Zainab Zaidi, Rohan Dandage, Dhanasekaran Shanmugam and Kausik Chakraborty ()
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Kanika Verma: CSIR-Institute of Genomics and Integrative Biology
Kanika Saxena: CSIR-Institute of Genomics and Integrative Biology
Rajashekar Donaka: CSIR-Institute of Genomics and Integrative Biology
Aseem Chaphalkar: CSIR-Institute of Genomics and Integrative Biology
Manish Kumar Rai: CSIR-Institute of Genomics and Integrative Biology
Anurag Shukla: Academy of Scientific and Innovative Research, CSIR-HRDC
Zainab Zaidi: CSIR-Institute of Genomics and Integrative Biology
Rohan Dandage: CSIR-Institute of Genomics and Integrative Biology
Dhanasekaran Shanmugam: Academy of Scientific and Innovative Research, CSIR-HRDC
Kausik Chakraborty: CSIR-Institute of Genomics and Integrative Biology

Nature Communications, 2020, vol. 11, issue 1, 1-15

Abstract: Abstract Metabolic changes alter the cellular milieu; can this also change intracellular protein folding? Since proteostasis can modulate mutational buffering, if change in metabolism has the ability to change protein folding, arguably, it should also alter mutational buffering. Here we find that altered cellular metabolic states in E. coli buffer distinct mutations on model proteins. Buffered-mutants have folding problems in vivo and are differently chaperoned in different metabolic states. Notably, this assistance is dependent upon the metabolites and not on the increase in canonical chaperone machineries. Being able to reconstitute the folding assistance afforded by metabolites in vitro, we propose that changes in metabolite concentrations have the potential to alter protein folding capacity. Collectively, we unravel that the metabolite pools are bona fide members of proteostasis and aid in mutational buffering. Given the plasticity in cellular metabolism, we posit that metabolic alterations may play an important role in cellular proteostasis.

Date: 2020
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DOI: 10.1038/s41467-020-16804-6

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