Histone deacetylases control lysine acetylation of ribosomal proteins in rice - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Nucleic Acids Research Année : 2021

Histone deacetylases control lysine acetylation of ribosomal proteins in rice

Résumé

Abstract Lysine acetylation (Kac) is well known to occur in histones 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 expression system. Ribo-seq analysis revealed that the hda714 mutations resulted in increased ribosome stalling frequency. Collectively, the results uncover Kac as a functional posttranslational modification of r-proteins which is controlled by histone deacetylases, extending the role of Kac in gene expression to protein translational regulation.

Dates et versions

hal-04452035 , version 1 (12-02-2024)

Licence

Domaine public

Identifiants

Citer

Qiutao Xu, Qian Liu, Zhengting Chen, Yaping Yue, Yuan Liu, et al.. Histone deacetylases control lysine acetylation of ribosomal proteins in rice. Nucleic Acids Research, 2021, 49 (8), pp.4613-4628. ⟨10.1093/nar/gkab244⟩. ⟨hal-04452035⟩

Collections

UNIV-PARIS-SACLAY
5 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More