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Histone Khib and acetylation, dark-induced starvat

2-Hydroxyisobutyrylation in Arabidopsis thaliana

41 modifications in 40 peptides, found in 41 proteins

Experiment Details

Exp 137


Experimental Setup
Tissue12-Day-old seedlings - histone extraction
ConditionControl
PTM Enrichmentanti-2-hydroxyisobutyryllysine (PTM-801; PTM Biolabs)
MS InstrumentQ Exactive Plus
MS/MS Search Parameters
Protein DatabaseUniProt Ddatabase
Decoy StrategyReverse decoy
FDR Threshold1% FDR
Search Algorithm(s)MaxQuant (version 1.5.2.8)
PTM Site AllocationPTM score
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsAcetylation (Protein N-term)
Oxidation (M)
2-Hydroxyisobutyrylation (K)
Deamidation (NQ)
Other Information
CommentsTable S2.


Publication Information

Zheng et al., 2021

PubMed ID: 34165567

ProteomeXchange: PXD018017

Abstract

Nucleic Acids Res. 2021 Jul 21;49(13):7347-7360. doi: 10.1093/nar/gkab536.

Functional interplay of histone lysine 2-hydroxyisobutyrylation and acetylation 
in Arabidopsis under dark-induced starvation.

Zheng L(1)(2), Li C(1)(2), Ma X(1)(2), Zhou H(3), Liu Y(3), Wang P(4), Yang 
H(4), Tamada Y(5), Huang J(6), Wang C(7), Hu Z(7), Wang X(8), Wang G(8), Li 
H(1), Hu J(1), Liu X(4), Zhou C(3), Zhang Y(1)(2).

Author information:
(1)Hubei Key Laboratory of Embryonic Stem Cell Research, School of Basic 
Medicine, Taihe Hospital, Hubei University of Medicine, Shiyan 442000, China.
(2)Hubei Key Laboratory of Wudang Local Chinese Medicine Research, Academy of 
Bio-Medicine Research, Hubei University of Medicine, Shiyan 442000, China.
(3)Key Laboratory of Three Gorges Regional Plant Genetics & Germplasm 
Enhancement (CTGU) /Biotechnology Research Center, China Three Gorges 
University, Yichang 443002, China.
(4)Institute for Interdisciplinary Research, Jianghan University, Wuhan 430056, 
China.
(5)School of Engineering, Utsunomiya University, Utsunomiya 321-8585, Japan.
(6)Center for Genomics and Systems Biology, Department of Biology, New York 
University, New York 10003, USA.
(7)Center for Multi-Omics Research, Key Laboratory of Plant Stress Biology, 
State Key Laboratory of Cotton Biology, School of Life Science, Henan 
University, Kaifeng 475001, China.
(8)College of Life Sciences, Shaanxi Normal University, Xi'an Shaanxi 710119, 
China.

Lysine 2-hydroxyisobutyrylation (Khib) is a novel type of histone acylation 
whose prevalence and function in plants remain unclear. Here, we identified 41 
Khib sites on histones in Arabidopsis thaliana, which did not overlap with 
frequently modified N-tail lysines (e.g. H3K4, H3K9 and H4K8). Chromatin 
immunoprecipitation-sequencing (ChIP-seq) assays revealed histone Khib in 35% of 
protein-coding genes. Most Khib peaks were located in genic regions, and they 
were highly enriched at the transcription start sites. Histone Khib is highly 
correlated with acetylation (ac), particularly H3K23ac, which it largely 
resembles in its genomic and genic distribution. Notably, co-enrichment of 
histone Khib and H3K23ac correlates with high gene expression levels. Metabolic 
profiling, transcriptome analyses, and ChIP-qPCR revealed that histone Khib and 
H3K23ac are co-enriched on genes involved in starch and sucrose metabolism, 
pentose and glucuronate interconversions, and phenylpropanoid biosynthesis, and 
help fine-tune plant response to dark-induced starvation. These findings suggest 
that Khib and H3K23ac may act in concert to promote high levels of gene 
transcription and regulate cellular metabolism to facilitate plant adaption to 
stress. Finally, HDA6 and HDA9 are involved in removing histone Khib. Our 
findings reveal Khib as a conserved yet unique plant histone mark acting with 
lysine acetylation in transcription-associated epigenomic processes.

© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic 
Acids Research.

DOI: 10.1093/nar/gkab536
PMCID: PMC8287917
PMID: 34165567 [Indexed for MEDLINE]