N-alpha-terminal Acetylation of Histone H4 Regulates Arginine Methylation and Ribosomal DNA Silencing
dc.contributor.author | Schiza, V. | en |
dc.contributor.author | Molina-Serrano, D. | en |
dc.contributor.author | Kyriakou, DImitris | en |
dc.contributor.author | Hadjiantoniou, A. | en |
dc.contributor.author | Kirmizis, Antonis | en |
dc.creator | Schiza, V. | en |
dc.creator | Molina-Serrano, D. | en |
dc.creator | Kyriakou, DImitris | en |
dc.creator | Hadjiantoniou, A. | en |
dc.creator | Kirmizis, Antonis | en |
dc.date.accessioned | 2019-11-04T12:52:38Z | |
dc.date.available | 2019-11-04T12:52:38Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 1553-7390 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/53372 | |
dc.description.abstract | Post-translational modifications of histones play a key role in DNA-based processes, like transcription, by modulating chromatin structure. N-terminal acetylation is unique among the numerous histone modifications because it is deposited on the N-alpha amino group of the first residue instead of the side-chain of amino acids. The function of this modification and its interplay with other internal histone marks has not been previously addressed. Here, we identified N-terminal acetylation of H4 (N-acH4) as a novel regulator of arginine methylation and chromatin silencing in Saccharomyces cerevisiae. Lack of the H4 N-alpha acetyltransferase (Nat4) activity results specifically in increased deposition of asymmetric dimethylation of histone H4 arginine 3 (H4R3me2a) and in enhanced ribosomal-DNA silencing. Consistent with this, H4 N-terminal acetylation impairs the activity of the Hmt1 methyltransferase towards H4R3 in vitro. Furthermore, combinatorial loss of N-acH4 with internal histone acetylation at lysines 5, 8 and 12 has a synergistic induction of H4R3me2a deposition and rDNA silencing that leads to a severe growth defect. This defect is completely rescued by mutating arginine 3 to lysine (H4R3K), suggesting that abnormal deposition of a single histone modification, H4R3me2a, can impact on cell growth. Notably, the cross-talk between N-acH4 and H4R3me2a, which regulates rDNA silencing, is induced under calorie restriction conditions. Collectively, these findings unveil a molecular and biological function for H4 N-terminal acetylation, identify its interplay with internal histone modifications, and provide general mechanistic implications for N-alpha-terminal acetylation, one of the most common protein modifications in eukaryotes. © 2013 Schiza et al. | en |
dc.source | PLoS Genetics | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84884694093&doi=10.1371%2fjournal.pgen.1003805&partnerID=40&md5=1bd9b51b17597c8c0f4f485be7521f72 | |
dc.subject | article | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | Mutation | en |
dc.subject | cell growth | en |
dc.subject | enzyme activity | en |
dc.subject | gene silencing | en |
dc.subject | growth disorder | en |
dc.subject | arginine | en |
dc.subject | protein interaction | en |
dc.subject | amino terminal sequence | en |
dc.subject | Saccharomyces cerevisiae | en |
dc.subject | amino acid substitution | en |
dc.subject | enzyme induction | en |
dc.subject | Protein Processing, Post-Translational | en |
dc.subject | Histones | en |
dc.subject | lysine | en |
dc.subject | methylation | en |
dc.subject | chromatin | en |
dc.subject | Substrate Specificity | en |
dc.subject | histone modification | en |
dc.subject | caloric restriction | en |
dc.subject | histone acetyltransferase | en |
dc.subject | histone H4 | en |
dc.subject | ribosome DNA | en |
dc.subject | Acetylation | en |
dc.subject | Acetyltransferases | en |
dc.subject | arginine methylation | en |
dc.subject | DNA, Ribosomal | en |
dc.subject | enzyme metabolism | en |
dc.subject | fungus growth | en |
dc.subject | histone acetylation | en |
dc.subject | Hmt1 methyltransferase | en |
dc.subject | Nat4 acetyltransferase | en |
dc.title | N-alpha-terminal Acetylation of Histone H4 Regulates Arginine Methylation and Ribosomal DNA Silencing | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1371/journal.pgen.1003805 | |
dc.description.volume | 9 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Βιολογικών Επιστημών / Department of Biological Sciences | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :18</p> | en |
dc.source.abbreviation | PLoS Genet. | en |
dc.contributor.orcid | Kirmizis, Antonis [0000-0002-3748-8711] | |
dc.gnosis.orcid | 0000-0002-3748-8711 |
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