Dataset Information

Global profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis

ABSTRACT: Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them share a common GCN5-related N-acetyltransferase (GNAT) domain. Although recent reports indicate that both NTA and KA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylations and why these modifications are that frequent in this organelle. Searches for new putative NAT and KAT genes in Arabidopsis thaliana illuminate a common pool of ten putative candidates, displaying a number of unique features both at the level of conserved key residues and motifs. Here, we show that eight out of the ten candidates are associated with the plastids. In vivo investigation based on global quantitative mass spectrometry of these enzymes revealed that they exhibit a number of unique features, supporting both NAT and KAT activities of the plastids. All identified enzymes show distinct KAT substrate specificity and display unexpected relaxed NAT substrate specificity, each with differences in terms of NTA yields and preferred substrates. Together, this study reveals an unexpected multitasking protein modification machinery dedicated to the plastids of plant. We suggest that this machinery likely evolved to support specific needs of this organelle.

ORGANISM(S): Escherichia Coli

SUBMITTER: Iris Finkemeyer

PROVIDER: PXD015875 | JPOST Repository | Tue Jul 07 00:00:00 BST 2020

REPOSITORIES: jPOST

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Dataset's files

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			Action	DRS
	171012_C17_034_QHF_PTM_Rev01_%2317_042_JMU06_K1.raw	Raw
	171012_C17_034_QHF_PTM_Rev01_%2317_042_JMU06_K2.raw	Raw
	171012_C17_034_QHF_PTM_Rev01_%2317_042_JMU06_K3.raw	Raw
	171012_C17_034_QHF_PTM_Rev01_%2317_042_JMU06_i1.raw	Raw
	171012_C17_034_QHF_PTM_Rev01_%2317_042_JMU06_i2.raw	Raw

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Publications

Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.

Bienvenut Willy V WV Brünje Annika A Boyer Jean-Baptiste JB Mühlenbeck Jens S JS Bernal Gautier G Lassowskat Ines I Dian Cyril C Linster Eric E Dinh Trinh V TV Koskela Minna M MM Jung Vincent V Seidel Julian J Schyrba Laura K LK Ivanauskaite Aiste A Eirich Jürgen J Hell Rüdiger R Schwarzer Dirk D Mulo Paula P Wirtz Markus M Meinnel Thierry T Giglione Carmela C Finkemeier Iris I

Molecular systems biology 20200701 7

Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All cha ...[more]

PMID: 32633465

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Project description:Reversible protein acetylation provides a central mechanism for controlling gene expression and cellular signaling events. It is governed by the antagonistic commitment of two enzymes families: the histone acetyltransferases (HATs) and the histone deacetylases (HDACs). HDAC4, like its class IIa counterparts, is a potent transcriptional repressor through interactions with tissue-specific transcription factors via its N-terminal domain. Whilst the lysine deacetylase activity of the class IIa HDACs is much less potent than that of the class I enzymes, HDAC4 has been reported to influence protein deacetylation through its interaction with HDAC3. To investigate the influence of HDAC4 on protein acetylation, we employed the unbiased AcetylScan proteomic screen. We identified many proteins known to be modified by acetylation, but found that the absence of HDAC4 had no effect on the acetylation profile of the murine neonate brain. This is consistent with the biochemical data suggesting that HDAC4 may not function as a lysine deacetylase, but these in vivo data do not support the previous report showing that the enzymatic activity of HDAC3 might be modified by its interaction with HDAC4. To complement this work, we used Affymetrix arrays to investigate the effect of HDAC4 knock-out on the transcriptional profile of the postnatal murine brain. There was no effect on global transcription, consistent with the absence of a differential histone acetylation profile. Validation of the array data by Taq-man qPCR indicated that only protamine 1 and Igfbp6 mRNA levels were increased by more than one-fold and only CamK4 was decreased. The lack of a major effect on the transcriptional profile is consistent with the cytoplasmic location of HDAC4 in the P3 murine brain. mRNA expression analysis was performed by microarray in 3-day-old HDAC4 KO pups and WT littermates. Ten samples were analysed for each genotype. Microarray quality control was performed using the software package provided on RACE (http://race.unil.ch).