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SIRT5 variants from patients with mitochondrial disease are associated with reduced SIRT5 stability and activity, but not with neuropathology

Yuan, T.; Kumar, S.; Skinner, M. E.; Victor-Joseph, R.; Abuaita, M.; Keijer, J.; Zhang, J.; Kunkel, T.; Liu, Y.; Petrunak, E.; Saunders, T.; Lieberman, A. P.; Stuckey, J. A.; Neamati, N.; AlMurshedi, F.; Alfadhel, M.; Spelbrink, J. N.; Rodenburg, R.; de Boer, V. C. J.; Lombard, D. B.

2023-12-08 genetics
10.1101/2023.12.06.570371 bioRxiv
Show abstract

SIRT5 is a sirtuin deacylase that represents the major activity responsible for removal of negatively-charged lysine modifications, in the mitochondrial matrix and elsewhere in the cell. In benign cells and mouse models, under basal non-stressed conditions, the phenotypes of SIRT5 deficiency are generally quite subtle. Here, we identify two homozygous SIRT5 variants in human patients suffering from severe mitochondrial disease. Both variants, P114T and L128V, are associated with reduced SIRT5 protein stability and impaired biochemical activity, with no evidence of neomorphic or dominant negative properties. The crystal structure of the P114T enzyme was solved and shows only subtle deviations from wild-type. Via CRISPR-Cas9, we generate a mouse model that recapitulates the human P114T mutation; homozygotes show reduced SIRT5 levels and activity, but no obvious metabolic abnormalities, neuropathology or other gross evidence of severe disease. We conclude that these human SIRT5 variants most likely represent severe hypomorphs, and are likely not the primary pathogenic cause of the neuropathology observed in the patients.

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