蛋白去乙酰化酶调控核糖体蛋白的机制获揭示

　　Lysine acetylation （Kac� is well known to occur in histo nes for chromatin function and epigenetic regulation. In addition to histones, Kac is also detected in a large number of proteins with diverse biological functions. However, Kac function and regulatory mechanism for most proteins are unclear. In this work, we studied mutation effects of rice genes encoding cytoplasm-localized histone deacetylases （HDAC� on protein acetylome and found that the HDAC protein HDA714 was a major deacetylase of the rice non-histone proteins including many ribosomal proteins （r-proteins� and translation factors that were extensively acetylated. HDA714 loss-of-function mutations increased Kac levels but reduced abundance of r-proteins. In vitro and in vivo experiments showed that HDA714 interacted with r-proteins and reduced their Kac. Substitutions of lysine by arginine （depleting Kac� in several r-proteins enhance, while mutations of lysine to glutamine （mimicking Kac� decrease their stability in transient ex pression system. Ribo-seq analysis revealed that the hda714 mutations resulted in increased ribosome stalling frequency. Collectively, the results uncover Kac as a functio nal posttranslatio nal modification of r-proteins which is co ntrolled by histone deacetylases, extending the role of Kac in gene ex pression to protein translatio nal regulation.

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