<i>Arabidopsis</i> downy mildew effector HaRxL106 suppresses plant immunity by binding to RADICAL‐INDUCED CELL DEATH1

Wirthmueller, Lennart; Asai, Shuji; Rallapalli, Ghanasyam; Sklenář, Jan; Fabro, Georgina; Kim, Dae Sung; Lintermann, Ruth; Jaspers, Pinja; Wrzaczek, Michael; Kangasjärvi, Jaakko; MacLean, Daniel; Menke, Frank L.H.; Banfield, Mark J.; Jones, Jonathan D. G.

doi:10.1111/nph.15277

Cited by 53 publications

(70 citation statements)

References 90 publications

(139 reference statements)

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“…The other residues involved in NAD + binding are conserved in active PARPs, regardless of whether activity is mono-or poly-ADP ribosylation. By contrast, the human zinc finger antiviral protein (HsZAP, or PARP13) and Arabidopsis RCD1 lack two or more of the NAD + -binding residues and are catalytically inactive (Karlberg et al, 2015;Wirthmueller et al, 2018). In TASOR the key residues required for catalysis are even more degenerated than in ZAP or RCD1: all but one of them are replaced by hydrophobic amino acids ( Fig.…”

Section: Tasor Duf3715 Is a Parp Domainmentioning

confidence: 99%

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

Douse

Tchasovnikarova

Timms

et al. 2020

Preprint

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stability; histone H3 lysine 9 methylation (H3K9me3); transposable element (TE); long interspersed nuclear element-1 (LINE-1); poly-ADP ribose polymerase (PARP); RNA-binding protein; RNA-induced transcriptional silencing; CUT&RUN; CUT&Tag; genome profiling SummaryThe Human Silencing Hub (HUSH) complex epigenetically represses retroviruses, transposons and genes in vertebrates. HUSH therefore maintains genome integrity and is central in the interplay between intrinsic immunity, transposable elements and transcriptional regulation. Comprising three subunits -TASOR, MPP8 and Periphilin -HUSH regulates SETDB1-dependent deposition of the transcriptionally repressive epigenetic mark H3K9me3 and recruits MORC2 to modify local chromatin structure. However the mechanistic roles of each HUSH subunit remain undetermined. Here we show that TASOR lies at the heart of HUSH, providing a platform for assembling the other subunits. Targeted epigenomic profiling supports the model that TASOR binds and regulates H3K9me3 specifically over LINE-1 repeats and other repetitive exons in transcribed genes. We find TASOR associates with several components of the nuclear RNA processing machinery and its modular domain architecture bears striking similarities to that of Chp1, the central component of the yeast RNA-induced transcriptional silencing (RITS) complex. Together these observations suggest that an RNA intermediate may be important for HUSH activity. We identify the TASOR domains necessary for HUSH assembly and transgene repression. Structural and genomic analyses reveal that TASOR contains a poly-ADP ribose polymerase (PARP) domain dispensable for assembly and chromatin localization, but critical for epigenetic regulation of target elements. This domain contains a degenerated and obstructed active site and has hence lost catalytic activity. Together our data demonstrate that TASOR is a pseudo-PARP critical for HUSH complex assembly and H3K9me3 deposition over its genomic targets.

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Section: Tasor Duf3715 Is a Parp Domainmentioning

confidence: 99%

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

Douse

Tchasovnikarova

Timms

et al. 2020

Preprint

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“…The interdomain regions of RCD1 are intrinsically disordered regions (IDRs), which likely provides flexibility in assuming the final overall protein conformation. RCD1 and its paralog, SRO1 (SIMILAR TO RCD ONE 1), can form homo-and heterodimers (Wirthmueller et al, 2018) and can be considered essential proteins since the rcd1 sro1 double mutant is not viable under standard growth conditions (Jaspers et al, 2009;Teotia & Lamb, 2011). In plants, the RST-domain is unique to the RCD1-SRO protein family and TAF4 proteins (Jaspers et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis poly(ADP-ribose)-binding protein RCD1 interacts with Photoregulatory Protein Kinases in nuclear bodies

Vainonen

Shapiguzov

Krasensky-Wrzaczek

et al. 2020

Preprint

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AbstractContinuous reprograming of gene expression in response to environmental signals in plants is achieved through signaling hub proteins that integrate external stimuli and transcriptional responses. RADICAL-INDUCED CELL DEATH1 (RCD1) functions as a nuclear hub protein, which interacts with a variety of transcription factors with its C-terminal RST domain and thereby acts as a co-regulator of numerous plant stress reactions. Here a previously function for RCD1 as a novel plant PAR reader protein is shown; RCD1 functions as a scaffold protein, which recruits transcription factors to specific locations inside the nucleus in PAR-dependent manner. The N-terminal WWE- and PARP-like domains of RCD1 bind poly(ADP-ribose) (PAR) and determine its localization to nuclear bodies (NBs), which is prevented by chemical inhibition of PAR synthesis. RCD1 also binds and recruits Photoregulatory Protein Kinases (PPKs) to NBs. The PPKs, which have been associated with circadian clock, abscisic acid, and light signaling pathways, phosphorylate RCD1 at multiple sites in the intrinsically disordered region between the WWE- and PARP-like-domains, which affects the stability and function of RCD1 in the nucleus. Phosphorylation of RCD1 by PPKs provides a mechanism where turnover of a PAR-binding transcriptional co-regulator is controlled by nuclear phosphorylation signaling pathways.

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“…In the last decade, lots of progress has been made on researches of CK1s from plants, especially Arabidopsis. The four MUT9-LIKE KINASEs (MLK1-4) have revealed to collectively impact Arabidopsis growth and development by involving in multiple physiological processes [5][6][7][8][9]. Previously, we found that the mlk1 mlk2 double mutant with pleiotropic defects including dwarfism, altered leaf shape and low fertility, was hypersensitive to osmotic stresses [10], suggesting the essentiality for plant growth and stress response.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, MLKs, also described as Arabidopsis EL1-like (AEL) proteins, were documented to phosphorylate ABA signal receptors PYRABACTIN RESISTANCE/PYR-LIKE (PYR/PYL) proteins to promote their degradation by ubiquitination, and triple mutants of mlks were hypersensitive to ABA treatment due to eliminated ABA responses [8]. Interestingly, one of the triple mutants, mlk1,3,4, showed elevated level of salicylic acid (SA)-induced defense marker genes, and MLKs were identified as interacting proteins with RADICAL-INDUCED CELL DEATH1 (RCD1), a positive regulator of SA signaling [7]. Taken together, Arabidopsis MLKs collectively play critical roles in diverse biological processes including stress response, light signaling and immunity.…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis MLK3, a Plant-specific Casein Kinase 1, Negatively Regulated Flowering and Phosphorylated Histone H3 in vivo

Wang

Jia²,

Zhang

et al. 2019

Preprint

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Background: Casein kinase 1 (CK1) family members are highly conserved serine/threonine kinase present in most eukaryotes with multiple biological functions. Arabidopsis MUT9-like kinases ( MLKs ) belong to a clade CK1 specific to the plant kingdom and have been implicated collectively in modulating flowering related processes. Three of the four MLKs ( MLK1/2/4 ) have been characterized, however, little is known about MLK3 , the most divergent MLKs.Results: We demonstrated that compared with wild type, mlk3 , a truncated MLK3 , flowered slightly early under long day conditions and ectopic expression of MLK3 rescued the morphological defects of mlk3 , indicating that MLK3 negatively regulates flowering. GA 3 application accelerated flowering of both wild type and mlk3 , suggesting that mlk3 had normal GA response. The recombinant MLK3-GFP was localized in the nucleus exclusively. In vitro kinase assay revealed that the nuclear protein MLK3 phosphorylated histone 3 at threonine 3 (H3T3ph). Mutation of a conserved catalytic residue (Lysine 175) abolished the kinase activity and resulted in failure to complement the early flowering phenotype of mlk3 . Interestingly, the global level of H3T3 phosphorylation in mlk3 did not differ significantly from wild type, suggesting the redundant roles of MLKs in flowering regulation. The transcriptomic analysis demonstrated that 425 genes significantly altered expression level in mlk3 relative to wild type. The mlk3 mlk4 double mutant generated by crossing mlk3 with mlk4 , a loss-offunction mutant of MLK4 showing late flowering, flowered between the two parental lines, suggesting that MLK3 played an antagonistic role to MLK4 in plant transition to flowering. Conclusions: A serine/threonine kinase encoding gene MLK3 is a casein kinase 1 specific to the plant species and represses flowering slightly. MLK3 located in nucleus catalyzes the phosphorylation of histone H3 at threonine 3 in vitro and an intact lysine residue (K175) is indispensible for the kinase activity. This study sheds new light on the delicate control of flowering by the plant-specific CK1 in Arabidopsis.

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Arabidopsis downy mildew effector HaRxL106 suppresses plant immunity by binding to RADICAL‐INDUCED CELL DEATH1

Cited by 53 publications

References 90 publications

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

Arabidopsis poly(ADP-ribose)-binding protein RCD1 interacts with Photoregulatory Protein Kinases in nuclear bodies

Arabidopsis MLK3, a Plant-specific Casein Kinase 1, Negatively Regulated Flowering and Phosphorylated Histone H3 in vivo

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