Search

Your search keyword '"Rayapuram, Naganand"' showing total 142 results
Start Over Author "Rayapuram, Naganand"
142 results on '"Rayapuram, Naganand"'

2. The wheat stem rust resistance gene Sr43 encodes an unusual protein kinase

Author

Yu, Guotai, Matny, Oadi, Gourdoupis, Spyridon, Rayapuram, Naganand, Aljedaani, Fatimah R., Wang, Yan L., Nürnberger, Thorsten, Johnson, Ryan, Crean, Emma E., Saur, Isabel M.-L., Gardener, Catherine, Yue, Yajuan, Kangara, Ngonidzashe, Steuernagel, Burkhard, Hayta, Sadiye, Smedley, Mark, Harwood, Wendy, Patpour, Mehran, Wu, Shuangye, Poland, Jesse, Jones, Jonathan D. G., Reuber, T. Lynne, Ronen, Moshe, Sharon, Amir, Rouse, Matthew N., Xu, Steven, Holušová, Kateřina, Bartoš, Jan, Molnár, István, Karafiátová, Miroslava, Hirt, Heribert, Blilou, Ikram, Jaremko, Łukasz, Doležel, Jaroslav, Steffenson, Brian J., and Wulff, Brande B. H.

Published
2023
Full Text
View/download PDF

3. Arabidopsis Actin-Binding Protein WLIM2A Links PAMP-Triggered Immunity and Cytoskeleton Organization.

Author

Manickam, Prabhu, Abulfaraj, Aala A., Alhoraibi, Hanna M., Veluchamy, Alaguraj, Almeida-Trapp, Marilia, Hirt, Heribert, and Rayapuram, Naganand

Abstract

Arabidopsis LIM proteins are named after the initials of three proteins Lin-11, Isl-1, and MEC-3, which belong to a class of transcription factors that play an important role in the developmental regulation of eukaryotes and are also involved in a variety of life processes, including gene transcription, the construction of the cytoskeleton, signal transduction, and metabolic regulation. Plant LIM proteins have been shown to regulate actin bundling in different cells, but their role in immunity remains elusive. Mitogen-activated protein kinases (MAPKs) are a family of conserved serine/threonine protein kinases that link upstream receptors to their downstream targets. Pathogens produce pathogen-associated molecular patterns (PAMPs) that trigger the activation of MAPK cascades in plants. Recently, we conducted a large-scale phosphoproteomic analysis of PAMP-induced Arabidopsis plants to identify putative MAPK targets. One of the identified phospho-proteins was WLIM2A, an Arabidopsis LIM protein. In this study, we investigated the role of WLIM2A in plant immunity. We employed a reverse-genetics approach and generated wlim2a knockout lines using CRISPR-Cas9 technology. We also generated complementation and phosphosite-mutated WLIM2A expression lines in the wlim2a background. The wlim2a lines were compromised in their response to Pseudomonas syringae Pst DC3000 but showed enhanced resistance to the necrotrophic fungus Botrytis cinereae. Transcriptome analyses of wlim2a mutants revealed the deregulation of immune hormone biosynthesis and signaling of salicylic acid (SA), jasmonic acid (JA), and ethylene (ET) pathways. The wlim2a mutants also exhibited altered stomatal phenotypes. Analysis of plants expressing WLIM2A variants of the phospho-dead or phospho-mimicking MAPK phosphorylation site showed opposing stomatal behavior and resistance phenotypes in response to Pst DC3000 infection, proving that phosphorylation of WLIM2A plays a crucial role in plant immunity. Overall, these data demonstrate that phosphorylation of WLIM2A by MAPKs regulates Arabidopsis responses to plant pathogens. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

5. A bivalent histone mark reader, AtDEK2 governs plant immunity

Author

Rayapuram, Naganand, primary, Alhoraibi, Hanna, additional, Alejandro-Martinez, Santiago, additional, Latrasse, David, additional, Mandal, Papita, additional, Faivre, Lea, additional, He, Xiaoning, additional, Mianza, Déborah Manza, additional, Abulfaraj, Aala, additional, Alhrabi, Siba, additional, Mariappan, Kiruthiga, additional, Artyukh, Olga, additional, Abdulhakim, Fatimah, additional, Aljedaani, Fatimah, additional, David, Stephan, additional, Almeida-Trapp, Marilia, additional, Bigeard, Jean, additional, Pflieger, Delphine, additional, Fischle, Wolfgang, additional, Arold, Stefan, additional, Colcombet, Jean, additional, Schubert, Daniel, additional, Benhamed, Moussa, additional, Blilou, Ikram, additional, and Hirt, Heribert, additional

Published
2024
Full Text
View/download PDF

7. Integrated multi‐omics and genetic analyses reveal molecular determinants underlying Arabidopsis snap33 mutant phenotype.

Author

Henchiri, Houda, Rayapuram, Naganand, Alhoraibi, Hanna M., Caïus, José, Paysant‐Le Roux, Christine, Citerne, Sylvie, Hirt, Heribert, Colcombet, Jean, Sturbois, Bénédicte, and Bigeard, Jean

Subjects
*MULTIOMICS, *PHENOTYPES, *ARABIDOPSIS, *MESSENGER RNA, *SALICYLIC acid, *PROTEIN receptors
Abstract

SUMMARY: The secretory pathway is essential for plant immunity, delivering diverse antimicrobial molecules into the extracellular space. Arabidopsis thaliana soluble N‐ethylmaleimide‐sensitive‐factor attachment protein receptor SNAP33 is a key actor of this process. The snap33 mutant displays dwarfism and necrotic lesions, however the molecular determinants of its macroscopic phenotypes remain elusive. Here, we isolated several new snap33 mutants that exhibited constitutive cell death and H2O2 accumulation, further defining snap33 as an autoimmune mutant. We then carried out quantitative transcriptomic and proteomic analyses showing that numerous defense transcripts and proteins were up‐regulated in the snap33 mutant, among which genes/proteins involved in defense hormone, pattern‐triggered immunity, and nucleotide‐binding domain leucine‐rich‐repeat receptor signaling. qRT‐PCR analyses and hormone dosages supported these results. Furthermore, genetic analyses elucidated the diverse contributions of the main defense hormones and some nucleotide‐binding domain leucine‐rich‐repeat receptor signaling actors in the establishment of the snap33 phenotype, emphasizing the preponderant role of salicylic acid over other defense phytohormones. Moreover, the accumulation of pattern‐triggered immunity and nucleotide‐binding domain leucine‐rich‐repeat receptor signaling proteins in the snap33 mutant was confirmed by immunoblotting analyses and further shown to be salicylic acid‐dependent. Collectively, this study unveiled molecular determinants underlying the Arabidopsis snap33 mutant phenotype and brought new insights into autoimmunity signaling. Significance Statement: SNAP33 is a key actor of secretion and the snap33 mutant exhibits dwarfism and necrotic lesions. The snap33 mutant is here further defined as an autoimmune mutant and molecular determinants of its macroscopic phenotypes are unveiled. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

8. Dynamics of ribosome composition and ribosomal protein phosphorylation in immune signaling in Arabidopsis thaliana

Author

Siodmak, Anna, primary, Martinez-Seidel, Federico, additional, Rayapuram, Naganand, additional, Bazin, Jeremie, additional, Alhoraibi, Hanna, additional, Gentry-Torfer, Dione, additional, Tabassum, Naheed, additional, Sheikh, Arsheed H, additional, Kise, José Kenyi González, additional, Blilou, Ikram, additional, Crespi, Martin, additional, Kopka, Joachim, additional, and Hirt, Heribert, additional

Published
2023
Full Text
View/download PDF

9. Salinity stress-induced phosphorylation of INDETERMINATE-DOMAIN 4 (IDD4) by MPK6 regulates plant growth adaptation in Arabidopsis

Author

Rawat, Anamika, primary, Völz, Ronny, additional, Sheikh, Arsheed, additional, Mariappan, Kiruthiga G., additional, Kim, Soon-Kap, additional, Rayapuram, Naganand, additional, Alwutayd, Khairiah M., additional, Alidrissi, Louai K., additional, Benhamed, Moussa, additional, Blilou, Ikram, additional, and Hirt, Heribert, additional

Published
2023
Full Text
View/download PDF

14. OXIDATIVE SIGNAL-INDUCIBLE1 induces immunity by coordinating N-hydroxypipecolic acid, salicylic acid, and camalexin synthesis

Author

Rawat, Anamika A., Hartmann, Michael, Harzen, Anne, Lugan, Raphael, Stolze, Sara Christina, Forzani, Celine, Abts, Laura, Reissenweber, Sophie, Rayapuram, Naganand, Nakagami, Hirofumi, Zeier, Jurgen, Hirt, Heribert, Rawat, Anamika A., Hartmann, Michael, Harzen, Anne, Lugan, Raphael, Stolze, Sara Christina, Forzani, Celine, Abts, Laura, Reissenweber, Sophie, Rayapuram, Naganand, Nakagami, Hirofumi, Zeier, Jurgen, and Hirt, Heribert

Abstract

Expression of OXIDATIVE SIGNAL-INDUCIBLE1 (OXI1) is induced by a number of stress conditions and regulates the interaction of plants with pathogenic and beneficial microbes. In this work, we generated Arabidopsis OXI1 knockout and genomic OXI1 overexpression lines and show by transcriptome, proteome, and metabolome analysis that OXI1 triggers ALD1, SARD4, and FMO1 expressions to promote the biosynthesis of pipecolic acid (Pip) and N-hydroxypipecolic acid (NHP). OXI1 contributes to enhanced immunity by induced SA biosynthesis via CBP60g-induced expression of SID2 and camalexin accumulation via WRKY33-targeted transcription of PAD3. OXI1 regulates genes involved in reactive oxygen species (ROS) generation such as RbohD and RbohF. OXI1 knock out plants show enhanced expression of nuclear and chloroplast genes of photosynthesis and enhanced growth under ambient conditions, while OXI1 overexpressing plants accumulate NHP, SA, camalexin, and ROS and show a gain-of-function (GOF) cell death phenotype and enhanced pathogen resistance. The OXI1 GOF phenotypes are completely suppressed when compromising N-hydroxypipecolic acid (NHP) synthesis in the fmo1 or ald1 background, showing that OXI1 regulation of immunity is mediated via the NHP pathway. Overall, these results show that OXI1 plays a key role in basal and effector-triggered plant immunity by regulating defense and programmed cell death via biosynthesis of salicylic acid, N-hydroxypipecolic acid, and camalexin.

Published
2023

16. Linker histone H1 modulates defense priming and immunity in plants

Author

Sheikh, Arsheed H, primary, Nawaz, Kashif, additional, Tabassum, Naheed, additional, Almeida-Trapp, Marilia, additional, Mariappan, Kiruthiga G, additional, Alhoraibi, Hanna, additional, Rayapuram, Naganand, additional, Aranda, Manuel, additional, Groth, Martin, additional, and Hirt, Heribert, additional

Published
2023
Full Text
View/download PDF

17. OXIDATIVE SIGNAL‐INDUCIBLE1 induces immunity by coordinating N‐hydroxypipecolic acid, salicylic acid, and camalexin synthesis

Author

Rawat, Anamika A., primary, Hartmann, Michael, additional, Harzen, Anne, additional, Lugan, Raphael, additional, Stolze, Sara Christina, additional, Forzani, Celine, additional, Abts, Laura, additional, Reißenweber, Sophie, additional, Rayapuram, Naganand, additional, Nakagami, Hirofumi, additional, Zeier, Jürgen, additional, and Hirt, Heribert, additional

Published
2022
Full Text
View/download PDF

19. Analysis of the Arabidopsiscoilinmutant reveals a positive role of AtCOILIN in plant immunity

Author

Abulfaraj, Aala A, primary, Alhoraibi, Hanna M, additional, Mariappan, Kiruthiga, additional, Bigeard, Jean, additional, Zhang, Huoming, additional, Almeida-Trapp, Marilia, additional, Artyukh, Olga, additional, Abdulhakim, Fatimah, additional, Parween, Sabiha, additional, Pflieger, Delphine, additional, Blilou, Ikram, additional, Hirt, Heribert, additional, and Rayapuram, Naganand, additional

Published
2022
Full Text
View/download PDF

22. The wheat stem rust resistance gene Sr43encodes an unusual protein kinase

Author

Yu, Guotai, Matny, Oadi, Gourdoupis, Spyridon, Rayapuram, Naganand, Aljedaani, Fatimah R., Wang, Yan L., Nürnberger, Thorsten, Johnson, Ryan, Crean, Emma E., Saur, Isabel M.-L., Gardener, Catherine, Yue, Yajuan, Kangara, Ngonidzashe, Steuernagel, Burkhard, Hayta, Sadiye, Smedley, Mark, Harwood, Wendy, Patpour, Mehran, Wu, Shuangye, Poland, Jesse, Jones, Jonathan D. G., Reuber, T. Lynne, Ronen, Moshe, Sharon, Amir, Rouse, Matthew N., Xu, Steven, Holušová, Kateřina, Bartoš, Jan, Molnár, István, Karafiátová, Miroslava, Hirt, Heribert, Blilou, Ikram, Jaremko, Łukasz, Doležel, Jaroslav, Steffenson, Brian J., and Wulff, Brande B. H.

Abstract

To safeguard bread wheat against pests and diseases, breeders have introduced over 200 resistance genes into its genome, thus nearly doubling the number of designated resistance genes in the wheat gene pool1. Isolating these genes facilitates their fast-tracking in breeding programs and incorporation into polygene stacks for more durable resistance. We cloned the stem rust resistance gene Sr43, which was crossed into bread wheat from the wild grass Thinopyrum elongatum2,3. Sr43encodes an active protein kinase fused to two domains of unknown function. The gene, which is unique to the Triticeae, appears to have arisen through a gene fusion event 6.7 to 11.6 million years ago. Transgenic expression of Sr43in wheat conferred high levels of resistance to a wide range of isolates of the pathogen causing stem rust, highlighting the potential value of Sr43in resistance breeding and engineering.

Published
2023
Full Text
View/download PDF

24. The Lys‐motif receptorLYK4mediates Enterobacter sp. SA187 triggered salt tolerance in Arabidopsis thaliana

Author

Rolli, Eleonora, primary, de Zélicourt, Axel, additional, Alzubaidy, Hanin, additional, Karampelias, Michael, additional, Parween, Sabiha, additional, Rayapuram, Naganand, additional, Han, Baoda, additional, Froehlich, Katja, additional, Abulfaraj, Aala A., additional, Alhoraibi, Hanna, additional, Mariappan, Kiruthiga, additional, Andrés‐Barrao, Cristina, additional, Colcombet, Jean, additional, and Hirt, Heribert, additional

Published
2021
Full Text
View/download PDF

27. Chromatin phosphoproteomics unravels a function for AT-hook motif nuclear localized protein AHL13 in PAMP-triggered immunity

Author

Agence Nationale de la Recherche (France), Centre Européen de Recherche en Biologie et en Médecine (France), King Abdullah University of Science and Technology, Institute of Plant Sciences Paris-Saclay, Rayapuram, Naganand, Jarad, Mai, Alhoraibi, Hanna M., Bigeard, Jean, Abulfaraj, Aala A., Völz, Ronny, Gayathri Mariappan, Kiruthiga, Almeida-Trapp, Marilia, Schlöffel, Maria, Lastrucci, Emmanuelle, Bonhomme, Ludovic, Gust, Andrea A., Mithöfer, Axel, Arold, Stefan T., Pflieger, Delphine, Hirt, Heribert, Agence Nationale de la Recherche (France), Centre Européen de Recherche en Biologie et en Médecine (France), King Abdullah University of Science and Technology, Institute of Plant Sciences Paris-Saclay, Rayapuram, Naganand, Jarad, Mai, Alhoraibi, Hanna M., Bigeard, Jean, Abulfaraj, Aala A., Völz, Ronny, Gayathri Mariappan, Kiruthiga, Almeida-Trapp, Marilia, Schlöffel, Maria, Lastrucci, Emmanuelle, Bonhomme, Ludovic, Gust, Andrea A., Mithöfer, Axel, Arold, Stefan T., Pflieger, Delphine, and Hirt, Heribert

Abstract

In many eukaryotic systems during immune responses, mitogen-activated protein kinases (MAPKs) link cytoplasmic signaling to chromatin events by targeting transcription factors, chromatin remodeling complexes, and the RNA polymerase machinery. So far, knowledge on these events is scarce in plants and no attempts have been made to focus on phosphorylation events of chromatin-associated proteins. Here we carried out chromatin phosphoproteomics upon elicitor-induced activation of Arabidopsis. The events in WT were compared with those in mpk3, mpk4, and mpk6 mutant plants to decipher specific MAPK targets. Our study highlights distinct signaling networks involving MPK3, MPK4, and MPK6 in chromatin organization and modification, as well as in RNA transcription and processing. Among the chromatin targets, we characterized the AT-hook motif containing nuclear localized (AHL) DNA-binding protein AHL13 as a substrate of immune MAPKs. AHL13 knockout mutant plants are compromised in pathogen-associated molecular pattern (PAMP)-induced reactive oxygen species production, expression of defense genes, and PAMP-triggered immunity. Transcriptome analysis revealed that AHL13 regulates key factors of jasmonic acid biosynthesis and signaling and affects immunity toward Pseudomonas syringae and Botrytis cinerea pathogens. Mutational analysis of the phosphorylation sites of AHL13 demonstrated that phosphorylation regulates AHL13 protein stability and thereby its immune functions.

Published
2021

28. AtCCMH, an essential component of the c-type cytochrome maturation pathway in Arabidopsis mitochondria, interacts with apocytochrome c

Author

Meyer, Etienne H., Giege, Philippe, Gelhaye, Eric, Rayapuram, Naganand, Ahuja, Umesh, Thony-Meyer, Linda, Grienenberger, Jean-Michel, and Bonnard, Geraldine

Subjects
Mitochondria -- Research, Mitochondria -- Genetic aspects, Cytochrome c -- Research, Science and technology
Abstract

The maturation of c-type cytochromes requires the covalent ligation of the heme cofactor to reduced cysteines of the CXXCH motif of apocytochromes. In contrast to mitochondria of other eukaryotes, plant mitochondria follow a pathway close to that found in [alpha]- and [gamma]-proteobacteria. We identified a nuclear-encoded protein, AtCCMH, the Arabidopsis thaliana ortholog of bacterial CcmH/CycL proteins. In bacteria, CcmH and the thioredoxin CcmG are components of a periplasmic thio-reduction pathway proposed to maintain the apocytochrome c cysteines in a reduced state. AtCCMH is located exclusively in mitochondria. AtCCMH is an integral protein of the inner membrane with the conserved RCXXC motif facing the intermembrane space. Reduction assays show that the cysteine thiols in the RCXXC motif of AtCCMH can form a disulfide bond that can be reduced by enzymatic thiol reductants. A reduced form of AtCCMH can reduce the intra-disulfide bridge of a model peptide of apocytochrome c. When expressed in Escherichia coil, AtCCMH coimmunoprecipitates with the bacterial CcmF, a proposed component of the heme lyase. Blue-native PAGE of mitochondrial membrane complexes reveals the colocalization of AtCCMH and [AtCcmF.sub.N2] in a 500-kDa complex. Yeast two-hybrid assays show an interaction between the AtCCMH intermembrane space domain and A. thaliana apocytochrome c. A. thaliana ccmh/ ccmh knockout plants show lethality at the torpedo stage of embryogenesis. Our results show that AtCCMH is an essential mitochondrial protein with characteristics consistent with its proposed apocytochrome c-reducing and heme lyase function. plant mitochondria | cytochrome c | disulfide reductase | heme lyase | embryo-lethal

Published
2005

31. The Lys‐motif receptor LYK4 mediates Enterobacter sp. SA187 triggered salt tolerance in Arabidopsis thaliana.

Author

Rolli, Eleonora, de Zélicourt, Axel, Alzubaidy, Hanin, Karampelias, Michael, Parween, Sabiha, Rayapuram, Naganand, Han, Baoda, Froehlich, Katja, Abulfaraj, Aala A., Alhoraibi, Hanna, Mariappan, Kiruthiga, Andrés‐Barrao, Cristina, Colcombet, Jean, and Hirt, Heribert

Subjects
ENTEROBACTER, PLANT-microbe relationships, DISEASE resistance of plants, SALT, ROOT growth
Abstract

Summary: Root endophytes establish beneficial interactions with plants, improving holobiont resilience and fitness, but how plant immunity accommodates beneficial microbes is poorly understood. The multi‐stress tolerance‐inducing endophyte Enterobacter sp. SA187 triggers a canonical immune response in Arabidopsis only at high bacterial dosage (>108 CFUs ml−1), suggesting that SA187 is able to evade or suppress the plant defence system at lower titres. Although SA187 flagellin epitopes are recognized by the FLS2 receptor, SA187‐triggered salt tolerance functions independently of the FLS2 system. In contrast, overexpression of the chitin receptor components LYK4 and LYK5 compromised the beneficial effect of SA187 on Arabidopsis, while it was enhanced in lyk4 mutant plants. Transcriptome analysis revealed that the role of LYK4 is intertwined with a function in remodelling defence responses with growth and root developmental processes. LYK4 interferes with modification of plant ethylene homeostasis by Enterobacter SA187 to boost salt stress resistance. Collectively, these results contribute to unlock the crosstalk between components of the plant immune system and beneficial microbes and point to a new role for the Lys‐motif receptor LYK4 in beneficial plant–microbe interaction. [ABSTRACT FROM AUTHOR]

Published
2022
Full Text
View/download PDF

32. Indeterminate-domain 4 4 (IDD4) coordinates immune responses with plant-growth in Arabidopsis thaliana

Author

Kim, Soon-Kap, Mi, Jianing, Rawat, Anamika A., Veluchamy, Alaguraj, Mariappan, Kiruthiga G., Rayapuram, Naganand, Daviere, Jean-Michel, Achard, Patrick, Blilou, Ikram, Al-Babili, Salim, Benhamed, Moussa, Volz, Ronny, and Hirt, Heribert

Subjects
salicylic-acglucosyltransferase, phosphoproteome profiling reveals, activated protein-kinases, receptor-like kinases, transcription factor, functional analyses, gene-expression, quantitative phosphoproteomics, innate immunity, dna-binding
Abstract

INDETERMINATE DOMAIN (IDD)/ BIRD proteins are a highly conserved plant-specific family of transcription factors which play multiple roles in plant development and physiology. Here, we show that mutation in IDD4/IMPERIAL EAGLE increases resistance to the hemi-biotrophic pathogen Pseudomonas syringae, indicating that IDD4 may act as a repressor of basal immune response and PAMP-triggered immunity. Furthermore, the idd4 mutant exhibits enhanced plant-growth indicating IDD4 as suppressor of growth and development. Transcriptome comparison of idd4 mutants and IDD4ox lines aligned to genome-wide IDD4 DNA-binding studies revealed major target genes related to defense and developmental-biological processes. IDD4 is a phospho-protein that interacts and becomes phosphorylated on two conserved sites by the MAP kinase MPK6. DNA-binding studies of IDD4 after flg22 treatment and with IDD4 phosphosite mutants show enhanced binding affinity to ID1 motif-containing promoters and its function as a transcriptional regulator. In contrast to the IDD4-phospho-dead mutant, the IDD4 phospho-mimicking mutant shows altered susceptibility to PstDC3000, salicylic acid levels and transcriptome reprogramming. In summary, we found that IDD4 regulates various hormonal pathways thereby coordinating growth and development with basal immunity. Author summary This work illustrates the involvement of the IDD family member 4 in the regulation of defense responses against hemibiotrophic pathogens and in processes governing plant growth. IDD4 is embedded in widely-ramified regulatory pathways and exerts transcriptional control of key factors that shape and balance growth with defense. Mutation in IDD4 and overexpression affect the plant shoot and root growth. At the same time, IDD4 acts as a repressor of innate immunity against the hemi-biotrophic pathogen Pst DC3000. IDD4 interacts with and is in vitro phosphorylated by the immune MAP kinase MPK6. Genome-wide IDD4 DNA-binding studies revealed subsets of direct targets contributing to various developmental processes and immunity. Chromatin-immunoprecipitation and DNA-shift experiments identified the ID1 motif as the prime target site of IDD4 and revealed that phospho-modifed IDD4 shows altered DNA binding ability and thereby gene expression and pathogen resistance. Overall, these results indicate that IDD4 links signal transduction to gene expression of genes involved in basal immunity and growth and development.

Published
2019

34. INDETERMINATE-DOMAIN 4 (IDD4) coordinates immune responses with plant-growth in Arabidopsis thaliana

Author

Völz, Ronny, primary, Kim, Soon-Kap, additional, Mi, Jianing, additional, Rawat, Anamika A., additional, Veluchamy, Alaguraj, additional, Mariappan, Kiruthiga G., additional, Rayapuram, Naganand, additional, Daviere, Jean-Michel, additional, Achard, Patrick, additional, Blilou, Ikram, additional, Al-Babili, Salim, additional, Benhamed, Moussa, additional, and Hirt, Heribert, additional

Published
2019
Full Text
View/download PDF

36. The Trihelix transcription factor GT2-like 1 (GTL1) promotes salicylic acid metabolism, and regulates bacterial-triggered immunity

Author

Völz, Ronny, primary, Kim, Soon-Kap, additional, Mi, Jianing, additional, Mariappan, Kiruthiga G., additional, Guo, Xiujie, additional, Bigeard, Jean, additional, Alejandro, Santiago, additional, Pflieger, Delphine, additional, Rayapuram, Naganand, additional, Al-Babili, Salim, additional, and Hirt, Heribert, additional

Published
2018
Full Text
View/download PDF

40. MAPK-triggered chromatin reprogramming by histone deacetylase in plant innate immunity

Author

Latrasse, David, Jégu, Teddy, Li, Huchen, de Zelicourt, Axel, Raynaud, Cécile, Legras, Stéphanie, Gust, Andrea, Samajova, Olga, Veluchamy, Alaguraj, Rayapuram, Naganand, Ramirez-Prado, Juan Sebastian, Kulikova, Olga, Colcombet, Jean, Bigeard, Jean, Genot, Baptiste, Bisseling, Ton, Benhamed, Moussa, Hirt, Heribert, Latrasse, David, Jégu, Teddy, Li, Huchen, de Zelicourt, Axel, Raynaud, Cécile, Legras, Stéphanie, Gust, Andrea, Samajova, Olga, Veluchamy, Alaguraj, Rayapuram, Naganand, Ramirez-Prado, Juan Sebastian, Kulikova, Olga, Colcombet, Jean, Bigeard, Jean, Genot, Baptiste, Bisseling, Ton, Benhamed, Moussa, and Hirt, Heribert

Abstract

Background: Microbial-associated molecular patterns activate several MAP kinases, which are major regulators of the innate immune response in Arabidopsis thaliana that induce large-scale changes in gene expression. Here, we determine whether microbial-associated molecular pattern-triggered gene expression involves modifications at the chromatin level. Results: Histone acetylation and deacetylation are major regulators of microbial-associated molecular pattern-triggered gene expression and implicate the histone deacetylase HD2B in the reprogramming of defence gene expression and innate immunity. The MAP kinase MPK3 directly interacts with and phosphorylates HD2B, thereby regulating the intra-nuclear compartmentalization and function of the histone deacetylase. Conclusions: By studying a number of gene loci that undergo microbial-associated molecular pattern-dependent activation or repression, our data reveal a mechanistic model for how protein kinase signaling directly impacts chromatin reprogramming in plant defense.

Published
2017

41. MAPK-triggered chromatin reprogramming by histone deacetylase in plant innate immunity

Author

Latrasse, David, primary, Jégu, Teddy, additional, Li, Huchen, additional, de Zelicourt, Axel, additional, Raynaud, Cécile, additional, Legras, Stéphanie, additional, Gust, Andrea, additional, Samajova, Olga, additional, Veluchamy, Alaguraj, additional, Rayapuram, Naganand, additional, Ramirez-Prado, Juan Sebastian, additional, Kulikova, Olga, additional, Colcombet, Jean, additional, Bigeard, Jean, additional, Genot, Baptiste, additional, Bisseling, Ton, additional, Benhamed, Moussa, additional, and Hirt, Heribert, additional

Published
2017
Full Text
View/download PDF

42. Proteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thaliana

Author

Bigeard, Jean, Rayapuram, Naganand, Bonhomme, Ludovic, Hirt, Heribert, Pflieger, Delphine, Unité de recherche en génomique végétale (URGV), Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), Spectroscopie, Modélisation, Interfaces pour L'Environnement et la Santé (SMiLES), Laboratoire de Chimie de la Matière Condensée de Paris (LCMCP), Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE - UMR 8587), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), and Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
Arabidopsis thaliana, Proteome, Molecular Sequence Data, Arabidopsis, plant, protein localization, chromatin assembly and disassembly, chemistry, Article, protein database, Databases, proteomics, nuclear protein, molecular biology, controlled study, Amino Acid Sequence, cell protein, protein motif, cellular distribution, chromatin associated protein, nonhuman, Arabidopsis protein, Arabidopsis Proteins, Protein, protein domain, Nuclear Proteins, protein function, phosphoprotein, Phosphoproteins, Chromatin, unclassified drug, enzyme activity, protein phosphorylation, protein stability, RNA processing, classification, protein analysis, molecular genetics, RNA, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], transcription regulation, metabolism
Abstract

International audience; The nucleus is the organelle where basically all DNA-related processes take place in eukaryotes, such as replication, transcription, and splicing as well as epigenetic regulation. The identification and description of the nuclear proteins is one of the requisites toward a comprehensive understanding of the biological functions accomplished in the nucleus. Many of the regulatory mechanisms of protein functions rely on their PTMs among which phosphorylation is probably one of the most important properties affecting enzymatic activity, interaction with other molecules, localization, or stability. So far, the nuclear and subnuclear proteome and phosphoproteome of the model plant Arabidopsis thaliana have been the subject of very few studies. In this work, we developed a purification protocol of Arabidopsis chromatin-associated proteins and performed proteomic and phosphoproteomic analyses identifying a total of 879 proteins of which 198 were phosphoproteins that were mainly involved in chromatin remodeling, transcriptional regulation, and RNA processing. From 230 precisely localized phosphorylation sites (phosphosites), 52 correspond to hitherto unidentified sites. This protocol and data thereby obtained should be a valuable resource for many domains of plant research.

Published
2014

48. Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets of ArabidopsisMitogen-Activated Protein Kinases (MAPKs) MPK3, MPK4, and MPK6*

Author

Rayapuram, Naganand, Bigeard, Jean, Alhoraibi, Hanna, Bonhomme, Ludovic, Hesse, Anne-Marie, Vinh, Joëlle, Hirt, Heribert, and Pflieger, Delphine

Abstract

In Arabidopsis, mitogen-activated protein kinases MPK3, MPK4, and MPK6 constitute essential relays for a variety of functions including cell division, development and innate immunity. Although some substrates of MPK3, MPK4 and MPK6 have been identified, the picture is still far from complete. To identify substrates of these MAPKs likely involved in cell division, growth and development we compared the phosphoproteomes of wild-type and mpk3, mpk4, and mpk6.To study the function of these MAPKs in innate immunity, we analyzed their phosphoproteomes following microbe-associated molecular pattern (MAMP) treatment. Partially overlapping substrates were retrieved for all three MAPKs, showing target specificity to one, two or all three MAPKs in different biological processes. More precisely, our results illustrate the fact that the entity to be defined as a specific or a shared substrate for MAPKs is not a phosphoprotein but a particular (S/T)P phosphorylation site in a given protein. One hundred fifty-two peptides were identified to be differentially phosphorylated in response to MAMP treatment and/or when compared between genotypes and 70 of them could be classified as putative MAPK targets. Biochemical analysis of a number of putative MAPK substrates by phosphorylation and interaction assays confirmed the global phosphoproteome approach. Our study also expands the set of MAPK substrates to involve other protein kinases, including calcium-dependent (CDPK) and sugar nonfermenting (SnRK) protein kinases.

Published
2018
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results