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Proximal cysteines enhance lysine acetylation of cytosolic proteins and are selected against in long-lived species

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dc.contributor.authorMurphy, MP
dc.contributor.orcidMurphy, Mike [0000-0003-1115-9618]
dc.date.accessioned2018-09-10T22:15:42Z
dc.date.available2018-09-10T22:15:42Z
dc.description.abstractAcetyl-CoA is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N-transfer of the acetyl moiety. Here, using modelled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ~10Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there was less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur.
dc.identifier.doi10.17863/CAM.27391
dc.identifier.issn2211-1247
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/280027
dc.language.isoeng
dc.publisherElsevier
dc.titleProximal cysteines enhance lysine acetylation of cytosolic proteins and are selected against in long-lived species
dc.typeArticle
dcterms.dateAccepted2018-06-06
prism.publicationNameCell Reports
pubs.funder-project-idMedical Research Council (MC_UU_00015/3)
pubs.funder-project-idWellcome Trust (110159/Z/15/Z)
rioxxterms.licenseref.startdate2018-06-06
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionAM

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