Correction: Phytoplasma-induced Changes in the Acetylome and Succinylome of Paulownia Tomentosa Provide Evidence for Involvement of Acetylated Proteins in Witches' Broom Disease.

Cao, Yabing; Gao, Fan; Wang, Zhe; Gu, Zhibin

doi:10.1074/mcp.aac119.001627

Cited by 2 publications

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“…(2020) P . tomentosa KacH, KacK, KacR, KacT, KacS, KacN, K∗∗∗∗∗∗∗∗KacK, K∗∗∗∗∗∗∗KacK, K∗∗∗∗∗∗KacK, Kac∗K, Kac∗∗K, KacAK, Kac∗R, Kac∗D, Kac∗E, AKacK Cao et al. (2019) T .…”

Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

“…Predictions of the protein secondary structures that surround Lys-acetylated lysines reveal distinct distribution patterns in different plant species. More than 60% of Lys-acetylated sites are found in coils followed by α-helix and β-strand regions ( Zhang et al., 2016 ; Jiang et al., 2018 ; Zhu et al., 2018 ; Cao et al., 2019 ; Yan et al., 2020 ), and more Lys-acetylated sites are found in the α helix than in the coil region in the Lys-acetylproteomes of O . sativa seeds ( He et al., 2016 ) and B .…”

Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

“…(2011) localized Lys-acetylated proteins to the nucleus, plasma membrane, and chloroplast, whereas the chromocenter was hypo-Lys-acetylated. Subcellular localization predictions reveal that the number of Lys-acetylated proteins varies across subcellular compartments among plant species, tissues, and developmental stages ( Fang et al., 2015 ; He et al., 2016 ; Xia et al., 2016 ; Xiong et al., 2016 ; Zhang et al., 2016 ; Zhen et al., 2016 ; Chen et al., 2018 ; Jiang et al., 2018 ; Li et al., 2018b , 2021b ; Meng et al., 2018 ; Xue et al., 2018 ; Zhou et al., 2018 ; Zhu et al., 2018 ; Cao et al., 2019 ; Yan et al., 2020 ; Liao et al., 2021 ) ( Figure 2 B). Almost 90% of Lys-acetylated proteins are located in the chloroplast, cytoplasm, nucleus, and mitochondria of plant cells.…”

Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

“…Expression of the HAT and HDAC genes in plants can be induced by biotic stresses, directly regulating cell LysAc and affecting host plant immunity and defense ( Zhou et al., 2005 ; Ding et al., 2012 ; Xu et al., 2015 ; Song and Walley, 2016 ). To date, analyses of plant Lys-acetylproteomes related to biotic stresses such as pests ( Melo-Braga et al., 2012 ), fungi ( Walley et al., 2018 ), phytoplasma ( Cao et al., 2019 ), and viruses ( Yuan et al., 2021 ) have been reported. Most studies have suggested that LysAc participates in plant responses to biotic stresses by remodeling the transcriptional network and regulating metabolic processes and immune response.…”

Section: Lysac In Plant Stress Responsesmentioning

confidence: 99%

“…To date, plant Lys-acetylproteome analyses have focused mainly on higher plants, including A . thaliana ( Finkemeier et al., 2011 ; Wu et al., 2011 ; Koenig et al., 2014 ; Hartl et al., 2017 ; Uhrig et al., 2017 ; Liu et al., 2018 ; Koskela et al., 2018 ; Bienvenut et al., 2020 ), Vitis vinifera ( Melo-Braga et al., 2012 ; Liu et al., 2019 ), Pisum sativum ( Smith-Hammond et al., 2014a ), Glycine max ( Smith-Hammond et al., 2014b ; Li et al., 2021a ), Oryza sativa ( Nallamilli et al., 2014 ; He et al., 2016 ; Xiong et al., 2016 ; Wang et al., 2017 ; Li et al., 2018a , 2018b ; Meng et al., 2018 ; Xue et al., 2018 ; Zhou et al., 2018 ), Fragaria ananassa ( Fang et al., 2015 ), Medicago truncatula ( Marx et al., 2016 ), Triticum aestivum ( Zhang et al., 2016 ; Zhu et al., 2018 ; Guo et al., 2020 ), Brachypodium distachyon ( Zhen et al., 2016 ), Picea asperata ( Xia et al., 2016 ), Camellia sinensis ( Xu et al., 2017 ; Jiang et al., 2018 ), Zea mays ( Walley et al., 2018 ; Yan et al., 2020 ), Kandelia candel ( Pan et al., 2018 ), Gossypium hirsutum ( Singh et al., 2020 ), Hibiscus cannabinus ( Chen et al., 2019 ), Paulownia tomentosa ( Cao et al., 2019 ), Petunia hybrida ( Zhao et al., 2020 ), Nicotiana benthamiana ( Yuan et al., 2021 ), Populus tremula × Populus alba ( Liao et al., 2021 ), Broussonetia papyrifera ( Li et al., 2021b ), and Phoebe zhennan ( Zhao et al., 2021 ) ( Table 1 ). By contrast, the Lys-acetylproteomes of lower plants are poorly studied and have been documented only in Phaeodactylum tricornutum ( Chen et al., 2018 ) and ...…”

Section: Introductionmentioning

confidence: 99%

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Advances in proteome-wide analysis of plant lysine acetylation

Xia

Kong

Song

et al. 2022

Plant Communications

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Lysine acetylation (LysAc) is a conserved and important post-translational modification (PTM) that plays a key role in plant physiological and metabolic processes. Based on advances in Lys-acetylated protein immunoenrichment and mass-spectrometric technology, LysAc proteomics studies have been performed in many species. Such studies have made substantial contributions to our understanding of plant LysAc, revealing that Lys-acetylated histones and nonhistones are involved in a broad spectrum of plant cellular processes. Here, we present an extensive overview of recent research on plant Lys-acetylproteomes. We provide in-depth insights into the characteristics of plant LysAc modifications and the mechanisms by which LysAc participates in cellular processes and regulates metabolism and physiology during plant growth and development. First, we summarize the characteristics of LysAc, including the properties of Lys-acetylated sites, the motifs that flank Lys-acetylated lysines, and the dynamic alterations in LysAc among different tissues and developmental stages. We also outline a map of Lys-acetylated proteins in the Calvin–Benson cycle and central carbon metabolism–related pathways. We then introduce some examples of the regulation of plant growth, development, and biotic and abiotic stress responses by LysAc. We discuss the interaction between LysAc and N α -terminal acetylation and the crosstalk between LysAc and other PTMs, including phosphorylation and succinylation. Finally, we propose recommendations for future studies in the field. We conclude that LysAc of proteins plays an important role in the regulation of the plant life cycle.

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Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

Section: Characteristics Of Lys-acetylated Proteinsmentioning

confidence: 99%

Section: Lysac In Plant Stress Responsesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Advances in proteome-wide analysis of plant lysine acetylation

Xia

Kong

Song

et al. 2022

Plant Communications

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Proteomic Analysis of Lysine Acetylation and Succinylation to Investigate the Pathogenicity of Virulent Pseudomonas syringae pv. tomato DC3000 and Avirulent Line Pseudomonas syringae pv. tomato DC3000 avrRpm1 on Arabidopsis thaliana

Ding,

Liu,

Yang

et al. 2024

Genes

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Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) is able to infect many economically important crops and thus causes substantial losses in the global agricultural economy. Pst DC3000 can be divided into virulent lines and avirulent lines. For instance, the pathogen effector avrRPM1 of avirulent line Pst-avrRpm1 (Pst DC3000 avrRpm1) can be recognized and detoxified by the plant. To further compare the pathogenicity mechanisms of virulent and avirulent Pst DC3000, a comprehensive analysis of the acetylome and succinylome in Arabidopsis thaliana was conducted following infection with virulent line Pst DC3000 and avirulent line Pst-avrRpm1. In this study, a total of 1625 acetylated proteins encompassing 3423 distinct acetylation sites were successfully identified. Additionally, 229 succinylated proteins with 527 unique succinylation sites were detected. A comparison of these modification profiles between plants infected with Pst DC3000 and Pst-avrRpm1 revealed significant differences. Specifically, modification sites demonstrated inconsistencies, with a variance of up to 10% compared to the control group. Moreover, lysine acetylation (Kac) and lysine succinylation (Ksu) displayed distinct preferences in their modification patterns. Lysine acetylation is observed to exhibit a tendency towards up-regulation in Arabidopsis infected with Pst-avrRpm1. Conversely, the disparity in the number of Ksu up-regulated and down-regulated sites was not as pronounced. Motif enrichment analysis disclosed that acetylation modification sequences are relatively conserved, and regions rich in polar acidic/basic and non-polar hydrophobic amino acids are hotspots for acetylation modifications. Functional enrichment analysis indicated that the differentially modified proteins are primarily enriched in the photosynthesis pathway, particularly in relation to light-capturing proteins. In conclusion, this study provides an insightful profile of the lysine acetylome and succinylome in A. thaliana infected with virulent and avirulent lines of Pst DC3000. Our findings revealed the potential impact of these post-translational modifications (PTMs) on the physiological functions of the host plant during pathogen infection. This study offers valuable insights into the complex interactions between plant pathogens and their hosts, laying the groundwork for future research on disease resistance and pathogenesis mechanisms.

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Correction: Phytoplasma-induced Changes in the Acetylome and Succinylome of Paulownia Tomentosa Provide Evidence for Involvement of Acetylated Proteins in Witches' Broom Disease.

Cited by 2 publications

References 0 publications

Advances in proteome-wide analysis of plant lysine acetylation

Advances in proteome-wide analysis of plant lysine acetylation

Proteomic Analysis of Lysine Acetylation and Succinylation to Investigate the Pathogenicity of Virulent Pseudomonas syringae pv. tomato DC3000 and Avirulent Line Pseudomonas syringae pv. tomato DC3000 avrRpm1 on Arabidopsis thaliana

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