Arabidopsis phytochrome A nuclear translocation is mediated by a far‐red elongated hypocotyl 1–importin complex

Helizon, Hanna; Rösler-Dalton, Jutta; Gasch, Philipp; Horsten, Silke von; Essen, Lars‐Oliver; Zeidler, Mathias

doi:10.1111/tpj.14107

Cited by 28 publications

(22 citation statements)

References 58 publications

(92 reference statements)

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“…From the perspective of P1-host protein interaction, VIP3/SKI8 turns over the 5′-fragment of RISC-cleaved target RNA, whereas TSN1, TSN2, and VSC are involved in mRNA decapping in stress granules and P-bodies (Branscheid et al 2015 ; Deyholos et al 2003 ; Gutierrez-Beltran et al 2015 ; Sorenson et al 2018 ; Xu and Chua 2009 ). Moreover, a MOS4 modifier, 2 IMPORTINs, and BIG5, which are involved in RNA splicing and RNA transportation, respectively, also interact with P1 Tu (Helizon et al 2018 ; Kitakura et al 2017 ; Luo et al 2013 ; Xu et al 2012 ). In addition, EMA1/SAD2 contains an importin-beta domain that negatively regulates miRNA activity (Wang et al 2011 ).…”

Section: Discussionmentioning

confidence: 99%

Investigation of the effects of P1 on HC-pro-mediated gene silencing suppression through genetics and omics approaches

Wei

Hong

et al. 2020

Bot Stud

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Background Posttranscriptional gene silencing (PTGS) is one of the most important mechanisms for plants during viral infection. However, viruses have also developed viral suppressors to negatively control PTGS by inhibiting microRNA (miRNA) and short-interfering RNA (siRNA) regulation in plants. The first identified viral suppressor, P1/HC-Pro, is a fusion protein that was translated from potyviral RNA. Upon infecting plants, the P1 protein itself is released from HC-Pro by the self-cleaving activity of P1. P1 has an unknown function in enhancing HC-Pro-mediated PTGS suppression. We performed proteomics to identify P1-interacting proteins. We also performed transcriptomics that were generated from Col-0 and various P1/HC-Pro-related transgenic plants to identify novel genes. The results showed several novel genes were identified through the comparative network analysis that might be involved in P1/HC-Pro-mediated PTGS suppression. Results First, we demonstrated that P1 enhances HC-Pro function and that the mechanism might work through P1 binding to VERNALIZATION INDEPENDENCE 3/SUPERKILLER 8 (VIP3/SKI8), a subunit of the exosome, to interfere with the 5 ′ -fragment of the PTGS-cleaved RNA degradation product. Second, the AGO1 was specifically posttranslationally degraded in transgenic Arabidopsis expressing P1/HC - Pro of turnip mosaic virus (TuMV) ( P1/HC Tu plant). Third, the comparative network highlighted potentially critical genes in PTGS, including miRNA targets, calcium signaling, hormone (JA, ET, and ABA) signaling, and defense response. Conclusion Through these genetic and omics approaches, we revealed an overall perspective to identify many critical genes involved in PTGS. These new findings significantly impact in our understanding of P1/HC-Pro-mediated PTGS suppression.

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Section: Discussionmentioning

confidence: 99%

Investigation of the effects of P1 on HC-pro-mediated gene silencing suppression through genetics and omics approaches

Wei

Hong

et al. 2020

Bot Stud

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“…The importance of OPM is previously highlighted by numerous missense mutations affecting this part of the protein [38,39]. The OPM of phytochromes has been reported to play roles in dimerization [40,41,42], nuclear localization [43,44], and signaling via protein-protein interaction with downstream components [14,45]. It has been suggested that the HKRD is a non-functional kinase domain due to the absence of key conserved residues within the histidine kinase domain [46].…”

Section: Domain Structure Of Plant Phytochromesmentioning

confidence: 99%

“…They interact directly with photoactivated phyA in the cytoplasm through their conserved C-terminal domain, and the phyA-FHY1/FHL complex is imported into the nucleus [62]. More recently, it is reported that the NLS of FHY1 is recognized by importin α (IMPα) independently of phyA, and phosphorylation on serine residues close to the NLS prevents FHY1 binding to IMPα [44]. In the nucleus, the photoactivated phytochromes interact with various downstream signaling components [45].…”

Section: Phytochrome-mediated Light Signaling In Plantsmentioning

confidence: 99%

“…More interestingly, it has been known that FHY1/FHL shows rapid R light-induced phosphorylation in a phyA-dependent manner [98,99]. More recently, it was shown that phosphorylation of serine residues near the NLS prevents FHY1 binding to IMPα [44]. Previously, the dissociation rate of phyA-FHY1/FHL complex is a principal determinant for the accumulation of phyA in the nucleus under FR light, i.e., phyA associates with FHY1/FHL in the cytoplasm but the phyA-FHY1/FHL complex should be dissociated in the nucleus for the phyA function [8].…”

Section: Protein Kinase Activities Of Plant Phytochromes In Plant mentioning

confidence: 99%

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Plant Phytochromes and their Phosphorylation

Hoang

Han

Kim

2019

IJMS

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Extensive research over several decades in plant light signaling mediated by photoreceptors has identified the molecular mechanisms for how phytochromes regulate photomorphogenic development, which includes degradation of phytochrome-interacting factors (PIFs) and inactivation of COP1-SPA complexes with the accumulation of master transcription factors for photomorphogenesis, such as HY5. However, the initial biochemical mechanism for the function of phytochromes has not been fully elucidated. Plant phytochromes have long been known as phosphoproteins, and a few protein phosphatases that directly interact with and dephosphorylate phytochromes have been identified. However, there is no report thus far of a protein kinase that acts on phytochromes. On the other hand, plant phytochromes have been suggested as autophosphorylating serine/threonine protein kinases, proposing that the kinase activity might be important for their functions. Indeed, the autophosphorylation of phytochromes has been reported to play an important role in the regulation of plant light signaling. More recently, evidence that phytochromes function as protein kinases in plant light signaling has been provided using phytochrome mutants displaying reduced kinase activities. In this review, we highlight recent advances in the reversible phosphorylation of phytochromes and their functions as protein kinases in plant light signaling.

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“…From the perspective of P1-host protein interaction, VIP3/SKI8 turns over the 5'-fragment of RISC-cleaved target RNA, whereas TSN1, TSN2, and VSC are involved in mRNA decapping in stress granules and P-bodies (Branscheid et al, 2015;Deyholos et al, 2003;Gutierrez-Beltran et al, 2015;Sorenson et al, 2018;Xu and Chua, 2009). Moreover, a MOS4 modi er, 2 IMPORTINs, and BIG5, which are involved in RNA splicing and RNA transportation, respectively, also interact with P1 Tu (Helizon et al, 2018;Kitakura et al, 2017;Luo et al, 2013;Xu et al, 2012). In addition, EMA1/SAD2 contains an importin-beta domain that negatively regulates miRNA activity (Wang et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Investigation of the effects of P1 on HC-Pro-mediated gene silencing suppression through genetics and omics approaches

Wei

Hong

et al. 2020

Preprint

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Background: Posttranscriptional gene silencing (PTGS) is one of the most important mechanisms for plants during viral infection. However, viruses have also developed viral suppressors to negatively control PTGS by inhibiting microRNA (miRNA) and short-interfering RNA (siRNA) regulation in plants. The first identified viral suppressor, P1/HC-Pro, is a fusion protein. Upon infecting plants, the P1 protein itself is released from HC-Pro by the self-cleaving activity of P1. P1 has an unknown function in enhancing HC-Pro-mediated PTGS suppression. We performed proteomics to identify P1-interacting proteins. We also performed transcriptomics that were generated from Col-0 and various P1/HC-Pro-related transgenic plants to identify novel genes. The results showed several novel genes were identified through the comparative network analysis that might be involved in P1/HC-Pro-mediated PTGS suppression. Results: First, we demonstrated that P1 enhances HC-Pro function and that the mechanism might work through P1 binding to VERNALIZATION INDEPENDENCE 3/SUPERKILLER 8 (VIP3/SKI8), a subunit of the exosome, to interfere with the 5'-fragment of the PTGS-cleaved RNA degradation product. Second, specifically the AGO1 was specifically posttranslationally degraded in transgenic Arabidopsis expressing P1/HC-Pro of turnip mosaic virus (TuMV) (P1/HCTu plant). Third, the comparative network highlighted potentially critical genes in PTGS, including miRNA targets, calcium signaling, hormone (JA, ET, and ABA) signaling, and defense response. Conclusion: Through these genetic and omics approaches, we revealed an overall perspective to identify many critical genes involved in PTGS. These new findings significantly impact in our understanding of P1/HC-Pro-mediated PTGS suppression.

show abstract

Arabidopsis phytochrome A nuclear translocation is mediated by a far‐red elongated hypocotyl 1–importin complex

Cited by 28 publications

References 58 publications

Investigation of the effects of P1 on HC-pro-mediated gene silencing suppression through genetics and omics approaches

Investigation of the effects of P1 on HC-pro-mediated gene silencing suppression through genetics and omics approaches

Plant Phytochromes and their Phosphorylation

Investigation of the effects of P1 on HC-Pro-mediated gene silencing suppression through genetics and omics approaches

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