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Journal Article

Mitochondrial chaperonin HSP60 is the apoptosis-related target for myrtucommulone

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Wielsch,  Natalie
Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society;

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Svatoš,  Aleš
Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society;

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Citation

Wiechmann, K., Müller, H., König, S., Wielsch, N., Svatoš, A., Jauch, J., et al. (2017). Mitochondrial chaperonin HSP60 is the apoptosis-related target for myrtucommulone. Cell Chemical Biology, 24(5), 614-623. doi:10.1016/j.chembiol.2017.04.008.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-8200-A
Abstract
The acylphloroglucinol myrtucommulone A (MC) causes mitochondrial dysfunctions by direct interference leading to apoptosis in cancer cells, but the molecular targets involved are unknown. Here, we reveal the chaperonin heat-shock protein 60 (HSP60) as a molecular target of MC that seemingly modulates HSP60-mediated mitochondrial functions. Exploiting an unbiased, discriminative protein fishing approach usingMC as bait and mitochondrial lysates from leukemic HL-60 cells as target source identified HSP60 as an MC-binding protein. MC prevented HSP60-mediated reactivation of denatured malate dehydrogenase in a protein refolding assay. Interference of MC with HSP60 was accompanied by aggregation of two proteins in isolated mitochondria under heat shock that were identified as Lon protease-like protein (LONP) and leucine-rich PPR motif-containing protein (LRP130). Together, our results reveal HSP60 as a direct target of MC, proposing MC as a valuable tool for studying HSP60 biology and for evaluating its value as a target in related diseases, such as cancer.