Arabidopsis EMSY-like (EML) histone readers are necessary for post-fertilization seed development, but prevent fertilization-independent seed formation

Milutinovic, Milica; Lindsey, Benson E.; Wijeratne, Asela J.; Hernandez, J. Marcela; Grotewold, Nikolas; Fernández, Virgínia; Grotewold, Erich; Brkljačić, Jelena

doi:10.1016/j.plantsci.2019.04.007

Cited by 12 publications

(10 citation statements)

References 69 publications

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“…We confirmed in vivo cleavage of ectopically expressed AtEML2, a nuclear histone reader protein ( 69 – 71 ). The protein was readily cleaved in TuMV-infected plants or in plants that coexpressed the TuMV or PPV proteases ( Fig.…”

Section: Discussionsupporting

confidence: 57%

“…We chose to test AtEML2, which was efficiently cleaved in vitro by both the PPV and TuMV proteases. AtEML2, a nuclear protein, belongs to a family of histone readers (also including AtEML1, AtEML3, and AtEML4) that have been associated with postfertilization seed development and pathogen resistance, including resistance to geminiviruses ( 69 – 71 ). The cleavage site is not conserved in AtEML1, AtEML3, or AtEML4.…”

Section: Resultsmentioning

confidence: 99%

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Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases

Xiao

Lord

Sanfaçon

2022

J Virol

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The NIa protease of potyviruses is a chymotrypsin-like cysteine protease related to the picornavirus 3C protease. It is also a multifunctional protein known to play multiple roles during virus infection. Picornavirus 3C proteases cleave hundreds of host proteins to facilitate virus infection. However, whether or not potyvirus NIa proteases cleave plant proteins has so far not been tested. Regular expression search using the cleavage site consensus sequence [EQN]xVxH[QE]/[SGTA] for the plum pox virus (PPV) protease identified 90-94 putative cleavage events in the proteomes of Prunus persica (a crop severely affected by PPV), Arabidopsis thaliana and Nicotiana benthamiana (two experimental hosts). In vitro processing assays confirmed cleavage of six A. thaliana and five P. persica proteins by the PPV protease. These proteins were also cleaved in vitro by the protease of turnip mosaic virus (TuMV), which has a similar specificity. We confirmed in vivo cleavage of a transiently expressed tagged version of AtEML2, an EMSY-like protein belonging to a family of nuclear histone readers known to be involved in pathogen resistance. Cleavage of AtEML2 was efficient and was observed in plants that co-expressed the PPV or TuMV NIa proteases or in plants that were infected with TuMV. We also show partial in vivo cleavage of AtDUF707, a membrane protein annotated as lysine ketoglutarate reductase trans-splicing protein. Although cleavage of the corresponding endogenous plant proteins remains to be confirmed, the results show that a plant virus protease can cleave host proteins during virus infection and highlight a new layer of plant-virus interactions. Importance Viruses are highly adaptive and use multiple molecular mechanisms to highjack or modify the cellular resources to their advantage. They must also counteract or evade host defense responses. One well-characterized mechanism used by vertebrate viruses is the proteolytic cleavage of host proteins to inhibit the activities of these proteins and/or to produce cleaved protein fragments that are beneficial to the virus infection cycle. Even though almost half of the known plant viruses encode at least one protease, it was not known whether plant viruses employ this strategy. Using an in silico prediction approach and the well-characterized specificity of potyvirus NIa proteases, we were able to identify hundreds of putative cleavage sites in plant proteins, several of which were validated by downstream experiments. It can be anticipated that many other plant virus proteases also cleave host proteins and that the identification of these cleavage events will lead to novel antiviral strategies.

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Section: Discussionsupporting

confidence: 57%

Section: Resultsmentioning

confidence: 99%

Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases

Xiao

Lord

Sanfaçon

2022

J Virol

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“…Other studies have also suggested that H3K36me3 and H3K4me2 are involved in auxin biosynthesis. The H3K36me3 histone mark readers EMSY-Like protein 1 (EML1) and EML3 in the Tudor/Agent family repress YUC10 expression during seed coat and endosperm development (Milutinovic et al, 2019 ). This is contrary to the common belief that H3K36me3 positively regulates gene transcription (Liu et al, 2010 ; Milutinovic et al, 2019 ), although the molecular mechanism remains unknown.…”

Section: The Repressive Histone Mark H3k27me3 Controls the Expression...mentioning

confidence: 99%

The roles of epigenetic modifications in the regulation of auxin biosynthesis

Wang

Luo

et al. 2022

Front. Plant Sci.

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Auxin is one of the most important plant growth regulators of plant morphogenesis and response to environmental stimuli. Although the biosynthesis pathway of auxin has been elucidated, the mechanisms regulating auxin biosynthesis remain poorly understood. The transcription of auxin biosynthetic genes is precisely regulated by complex signaling pathways. When the genes are expressed, epigenetic modifications guide mRNA synthesis and therefore determine protein production. Recent studies have shown that different epigenetic factors affect the transcription of auxin biosynthetic genes. In this review, we focus our attention on the molecular mechanisms through which epigenetic modifications regulate auxin biosynthesis.

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“…In Arabidopsis , the single Tudor domain protein EMSY-like 1 (EML1) functions as a plant-specific H3K4me2/3 reader, different from the case in humans that only double or tandem Tudor domains can recognize H3K4me2/3 ( Zhao et al, 2018 ), indicating a plant-specific recognition mode. EML1 can also recognize H3K36me3 ( Milutinovic et al, 2019 ) with a much weaker binding affinity for H3K36me3 than for H3K4me3 ( Zhao et al, 2018 ). The Tudor domain protein MSH6, a DNA mismatch repair protein, binds to H3K4me3 with a much weaker affinity than H3K36me3 in vitro ( Zhao et al, 2018 ).…”

Section: “Writers” “Readers” and “Erasers” For Histone H3 Lysine Methylationmentioning

confidence: 99%

Reprogramming of Histone H3 Lysine Methylation During Plant Sexual Reproduction

Fang

Shao

2021

Front. Plant Sci.

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Plants undergo extensive reprogramming of chromatin status during sexual reproduction, a process vital to cell specification and pluri- or totipotency establishment. As a crucial way to regulate chromatin organization and transcriptional activity, histone modification can be reprogrammed during sporogenesis, gametogenesis, and embryogenesis in flowering plants. In this review, we first introduce enzymes required for writing, recognizing, and removing methylation marks on lysine residues in histone H3 tails, and describe their differential expression patterns in reproductive tissues, then we summarize their functions in the reprogramming of H3 lysine methylation and the corresponding chromatin re-organization during sexual reproduction in Arabidopsis, and finally we discuss the molecular significance of histone reprogramming in maintaining the pluri- or totipotency of gametes and the zygote, and in establishing novel cell fates throughout the plant life cycle. Despite rapid achievements in understanding the molecular mechanism and function of the reprogramming of chromatin status in plant development, the research in this area still remains a challenge. Technological breakthroughs in cell-specific epigenomic profiling in the future will ultimately provide a solution for this challenge.

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Arabidopsis EMSY-like (EML) histone readers are necessary for post-fertilization seed development, but prevent fertilization-independent seed formation

Cited by 12 publications

References 69 publications

Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases

Proteolytic Processing of Plant Proteins by Potyvirus NIa Proteases

The roles of epigenetic modifications in the regulation of auxin biosynthesis

Reprogramming of Histone H3 Lysine Methylation During Plant Sexual Reproduction

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