{"id":110,"date":"2013-03-27T07:30:41","date_gmt":"2013-03-27T07:30:41","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=110"},"modified":"2020-03-21T16:39:11","modified_gmt":"2020-03-21T16:39:11","slug":"a-hecker","status":"publish","type":"page","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=110","title":{"rendered":"Hecker Arnaud"},"content":{"rendered":"<p><strong>Bio:<\/strong> I received\u00a0a Ph.D in Biology, Cellular and Molecular Biology\u00a0from the University of Burgundy (Dijon) in 2002. Under the supervision of Pr. Gilles Luquet, my research activities focused on the structure-function analysis\u00a0of Orchestin, a protein involved in a biomineralization process in the crustacea <em>Orchestia cavimana<\/em>. Later, I was hired in 2003\u00a0as non-permanent lecturer at the University of Burgundy (Dijon). Under the supervision of Dr. Fr\u00e9d\u00e9ric Marin, I was interested in\u00a0the biochemical characterization of proteins involved in the shell formation of the mollusk <em>Pina nobilis<\/em>. Then, I moved in 2004 to the Institute of Genetics and Microbiology (University of Paris-Sud XI). In\u00a0the team headed by Pr. Patrick Forterre,\u00a0my research activities focused in Archaea on deciphering the role and functions of KEOPS complex, a highly conserved complex essential for the maturation of the universal t6A tRNA modification. Finally, I joined the Stress Response and Redox regulation team\u00a0in September\u00a02010 as\u00a0assistant professor and became professor in September 2019.<\/p>\n<p><strong>Present research:<\/strong> My current work focuses on two main topics: the biochemical and structural analysis of glutathione transferases in plants and the study of some molecular actors involved in the host-pathogen interaction between the biotrophic rust fungus <em>Melampsora larici<\/em> and the tree <em>Populus trichocarpa<\/em>.<\/p>\n<p><strong>Publications <\/strong><strong>(for an up-to-date list, you can refer to the following links: <\/strong><a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=arnaud+hecker\"><strong>PubMed<\/strong><\/a><strong>, <\/strong><a href=\"https:\/\/orcid.org\/0000-0003-4511-5410\"><strong>ORCID<\/strong><\/a><strong>, <\/strong><a href=\"https:\/\/scholar.google.com\/citations?user=LzErFMkAAAAJ&amp;hl=fr&amp;oi=ao\"><strong>Google Scholar<\/strong><\/a><strong>, <\/strong><a href=\"https:\/\/www.researchgate.net\/profile\/Arnaud_Hecker\"><strong>ResearchGate<\/strong><\/a><strong> and <\/strong><a href=\"https:\/\/loop.frontiersin.org\/people\/175427\/overview\"><strong>Loop<\/strong><\/a><strong>)<\/strong><\/p>\n<p><strong>2020<\/strong><\/p>\n<p>Sylvestre-Gonon, E., Schwartz, M., Girardet, J.M., Hecker, A. and Rouhier, N. (2020). Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signaling in plants? <em>Phil. Trans. R. Soc. B<\/em>, under press.<\/p>\n<p><strong>2019<\/strong><\/p>\n<p>de Guillen, K., Lorrain, C., Tsan, P., Barthe, P., Petre, B., Saveleva, N, Rouhier, N., Duplessis, S., Padilla, A. and <strong>Hecker A. <\/strong>(2019). Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds. <em>Sci. Rep.<\/em> <strong>9<\/strong>:18084.<\/p>\n<p>Csisz\u00e1r, J., <strong>Hecker, A.<\/strong>, Labrou, N.E., Schr\u00f6der, P. and Riechers D.E. (2019). Editorial: Plant Glutathione Transferases: Diverse, Multi-Tasking Enzymes With Yet-to-Be Discovered Functions. <em>Front. Plant Sci.<\/em> <strong>10<\/strong>:1304.<\/p>\n<p>Pellegrin, C., Daguerre, Y., Ruytinx, J., Guinet, F., Kemppainen, M., Frey, N.F.D., Puech-Pag\u00e8s, V., <strong>Hecker, A.<\/strong>, Pardo, A.G., Martin, F.M. and Veneault-Fourrey, C. (2019). Laccaria bicolor MiSSP8 is a small-secreted protein decisive for the establishment of the ectomycorrhizal symbiosis. <em>Environ. Microbiol.<\/em> <strong>21<\/strong>:3765-3779.<\/p>\n<p>Sylvestre-Gonon, E., Law, S.R., Schwartz, M., Robe, K., Keech, O., Didierjean, C., Dubos, C., Rouhier, N. and <strong>Hecker, A.<\/strong> (2019). Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases. <em>Front. Plant. Sci.<\/em> <strong>10<\/strong>:608.<\/p>\n<p>Lorrain, C., Gon\u00e7alves Dos Santos, K.C., Germain, H., <strong>Hecker, A.<\/strong> and Duplessis, S. (2019). Advances in understanding obligate biotrophy in rust fungi. <em>New Phytol.<\/em> <strong>222<\/strong>:1190-1206.<\/p>\n<p><strong>2018<\/strong><\/p>\n<p>Lorrain, C., Marchal, C., Hacquard, S., Delaruelle, C., P\u00e9trowski, J., Petre, B., <strong>Hecker, A.<\/strong>, Frey, P. and Duplessis, S. (2018). The rust fungus Melampsora larici-populina expresses a conserved genetic program and distinct sets of secreted protein genes during infection of its two host plants, larch and poplar. <em>Mol. Plant Microbe Interact. <\/em><strong>31<\/strong>:695-706.<\/p>\n<p>Plomion, C., Aury, J.M., Amselem, J., Leroy, T., Murat, F.5., Duplessis, S., &#8230;, <strong>Hecker, A.<\/strong>, \u2026, Salse J. (2018). Oak genome reveals facets of long lifespan. <em>Nature Plants<\/em> <strong>4<\/strong>:440-452.<\/p>\n<p><strong>2017<\/strong><\/p>\n<p>G\u00fctle, D.D., Roret, T., <strong>Hecker, A.<\/strong>, Reski, R. and Jacquot,\u00a0J.P. (2017). Dithiol disulphide exchange in redox regulation of chloroplast enzymes in response to evolutionary and structural constraints. <em>Plant Sci.<\/em> <strong>255<\/strong>, 1-11.<\/p>\n<p>Shaikhali, J., Rouhier, N., <strong>Hecker, A.<\/strong>, Br\u00e4nnstr\u00f6m, K. and Wingsle, G. (2017). Covalent and non-covalent associations mediate MED28 homo-oligomerization, <em>J. Plant Biochem. Physiol.<\/em> <strong>5<\/strong>:189.<\/p>\n<p>P\u00e9geot, H., Mathiot, S., Perrot, T., Gense, F., <strong>Hecker, A.<\/strong>, Didierjean, C. and Rouhier, N. (2017). Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities. <em>FEBS J<\/em>. <strong>284<\/strong>:2442-2463.<\/p>\n<p><strong>2016<\/strong><\/p>\n<p>Schwartz, M., Didierjean, C., <strong>Hecker, A.<\/strong>, Girardet, J.M., Morel-Rouhier, M., Gelhaye, E. and Favier, F. (2016). Crystal Structure of <em>Saccharomyces cerevisiae<\/em> ECM4, a Xi-class glutathione transferase that reacts with glutathionyl-(hydro)quinones. <em>PLoS One<\/em> <strong>11<\/strong>, e0164678.<\/p>\n<p>G\u00fctle, D.D., Roret, T., M\u00fcller, S.J., Couturier, J., Lemaire, S.D., <strong>Hecker, A.<\/strong>, Dhalleine, T., Buchanan, B.B., Reski, R., Einsle, O. and Jacquot J.P. (2016). Chloroplast FBPase and SBPase are thioredoxin-linked enzymes with similar architecture but different evolutionary histories. <em>Proc. Natl. Acad. Sci. U.S.A.<\/em> <strong>113<\/strong>, 6779-6784.<\/p>\n<p>Petre, B., <strong>Hecker, A.<\/strong>, Germain, H., Tsan, P., Sklenar, J., Pelletier, G., S\u00e9guin, A., Duplessis, S. and Rouhier, N. (2016). The Poplar Rust-Induced Secreted Protein (RISP) Inhibits the growth of the leaf rust pathogen <em>Melampsora larici<\/em>\u2013<em>populina<\/em> and triggers cell culture alkalinisation. <em>Front. Plant Sci.<\/em> <strong>7<\/strong>, 97.<\/p>\n<p>Lallement, P.A., Roret, T., Tsan, P., Gualberto, J.M., Girardet, J.M., Didierjean, C., Rouhier, N. and <strong>Hecker, A.<\/strong> (2016). Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from <em>Populus trichocarpa<\/em>. <em>Biochem J.<\/em> <strong>473<\/strong>, 717-731.<\/p>\n<p>Jacquot, J.P., Couturier, J., Didierjean, C., Gelhaye, E., Morel-Rouhier, M., <strong>Hecker, A.<\/strong>, Plomion, C., G\u00fctle, D. and Rouhier, N. (2016). Structural and functional characterization of tree proteins involved in redox regulation: a new frontier in forest science. <em>Ann. For. Sci.<\/em> <strong>73<\/strong>, 119\u2013134.<\/p>\n<p><strong>2015<\/strong><\/p>\n<p>Lorrain, C., <strong>Hecker, A.<\/strong> and Duplessis, S. (2015). Effector-Mining in the Poplar Rust Fungus <em>Melampsora larici<\/em>\u2013<em>populina<\/em> secretome. <em>Front. Plant Sci.<\/em> <strong>6<\/strong>, 1051.<\/p>\n<p>Deroy, A., Saiag, F., Kebbi-Benkeder, Z., Touahri, N., <strong>Hecker, A.<\/strong>, Morel-Rouhier, M., Colin, F., Dumarcay, S., G\u00e9rardin, P. and Gelhaye, E. (2015). The GSTome reflects the chemical environment of white-rot fungi. <em>PLoS One<\/em> <strong>10<\/strong>, e0137083.<\/p>\n<p>Lallement, P.A., Meux, E., Gualberto, J.M., Dumarcay, S., Favier, F., Didierjean, C., Saul, F., Haouz, A., Morel-Rouhier, M., Gelhaye, E., Rouhier, N. and <strong>Hecker A. <\/strong>(2015). Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones. <em>FEBS Lett.<\/em> <strong>589<\/strong>, 37-44.<\/p>\n<p><strong>2014<\/strong><\/p>\n<p>P\u00e9geot, H., Koh, C.S., Petre, B., Mathiot, S., Duplessis, S., <strong>Hecker, A.<\/strong>, Didierjean, C. and Rouhier, N. (2014). The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1. <em>Front. Plant Sci.<\/em> <strong>5<\/strong>:712.<\/p>\n<p>Lallement, P.A., Brouwer, B., Keech, O., <strong>Hecker, A.<\/strong> and Rouhier, N. (2014). The still mysterious roles of cysteine-containing glutathione transferases in plants. <em>Front. Pharmacol.<\/em> <strong>5<\/strong>, 192.<\/p>\n<p>Thiaville, P.C., El Yacoubi, B., Perrochia, L., <strong>Hecker, A.<\/strong>, Prigent, M., Thiaville, J.J., Forterre, P., Namy, O., Basta, T. and de Cr\u00e9cy-Lagard V. (2014). Cross kingdom functional conservation of the core universally conserved threonylcarbamoyladenosine tRNA synthesis enzymes. <em>Eukaryot. Cell <\/em><strong>13<\/strong>, 1222-1231.<\/p>\n<p>Lallement, P.A., Meux, E., Gualberto, J.M., Prosper, P., Didierjean, C., Saul, F., Haouz, A., Rouhier, N. and <strong>Hecker, A.<\/strong> (2014). Structural and enzymatic insights into Lambda glutathione transferases from <em>Populus trichocarpa<\/em>, monomeric enzymes constituting an early divergent class specific to terrestrial plants. <em>Biochem. J.<\/em> <strong>462<\/strong>, 39-52.<\/p>\n<p><strong>2013<\/strong><\/p>\n<p>Jacquot, J.P.,\u00a0Dietz, K.J.,\u00a0Rouhier, N.,\u00a0Meux, E.,\u00a0Lallement, P.A.,\u00a0Selles, B. and\u00a0<strong>Hecker, A.<\/strong> (2013). Redox Regulation in Plants: Glutathione and \u201cRedoxin\u201d Related Families. I<em>n Oxidative Stress and Redox Regulation<\/em>, Jakob U. (Ed.), Springer, 213-231 (book chapter).<\/p>\n<p>Perrochia, L., Guetta, D., <strong>Hecker, A.<\/strong>, Forterre, P. and\u00a0Basta, T. (2013). Functional assignment of KEOPS\/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification. <em>Nucleic Acids Res.<\/em> <strong>41<\/strong>, 9484-9499.<\/p>\n<p>Perrochia, L., Crozat, E., <strong>Hecker, A.<\/strong>, Zhang, W., Bareille, J., Collinet, B., van Tilbeurgh, H., Forterre, P. and Basta, T. (2013). In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya. <em>Nucleic Acids Res.<\/em> <strong>41<\/strong>, 1953-1964.<\/p>\n<p>Couturier, J., Prosper, P., Winger, A.M., <strong>Hecker, A.<\/strong>, Hirasawa, M., Knaff, D., Gans, P., Jacquot, J.P., Navaza, A., Haouz, A. and Rouhier, N. (2013). In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima? <em>Antioxid. Redox Signal. <\/em><strong>18<\/strong>, 1613-1622.<\/p>\n<p><strong>2011<\/strong><\/p>\n<p>Hacquard, S., Petre, B., Frey, P., <strong>Hecker, A.<\/strong>, Rouhier, N. and Duplessis, S. (2011). The poplar-poplar rust interaction: insights from genomics and transcriptomics. <em>J. Pathog.<\/em> <strong>2011<\/strong>, 2011-716041.<\/p>\n<p><strong>2009<\/strong><\/p>\n<p>Oberto, J., Breuil, N., <strong>Hecker, A.<\/strong>, Farina, F., Brochier-Armanet, C., Culetto, E. and Forterre, P. (2009). Qri7\/OSGEPL, the mitochondrial version of the universal Kae1\/YgjD protein, is essential for mitochondrial genome maintenance. <em>Nucleic Acids Res.<\/em> <strong>37<\/strong>, 5343-5352.<\/p>\n<p>Muller, S., Urban, A., <strong>Hecker, A<\/strong>., Leclerc, F., Branlant, C. and Motorin, Y. (2009). Deficiency of the tRNATyr:\u03a835-synthase aPus7 in Archaea of the Sulfolobales order might be rescued by the H\/ACA sRNA-guided Machinery. <em>Nucleic Acids Res.<\/em> <strong>37<\/strong>, 1308-1322.<\/p>\n<p><strong>Hecker, A.<\/strong>, Graille, M., Madec, E., Gadelle, D., Le Cam, E., van Tilbeurgh, H. and Forterre, P. (2009). The universal Kae1 protein and the associated Bud32 kinase (PRPK), a mysterious protein couple probably essential for genome maintenance in Archaea and Eukarya. <em>Biochem. Soc. Trans.<\/em> <strong>37<\/strong>, 29-35.<\/p>\n<p><strong>2008<\/strong><\/p>\n<p><strong>Hecker, A.<\/strong>, Lopreiato, R., Graille, M., Collinet, B., Forterre, P., Libri, D. and van Tilbeurgh, H. (2008). Structure of the archaeal Kae1\/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC\/KEOPS subcomplex. <em>EMBO J.<\/em> <strong>27<\/strong>, 2340\u20132351.<\/p>\n<p><strong>2007<\/strong><\/p>\n<p><strong>Hecker, A.<\/strong>, Leulliot, N., Gadelle, D., Graille, M., Justome, A., Dorlet, P., Brochier, C., Quevillon-Cheruel, S., Le Cam, E., van Tilbeurgh, H. and Forterre, P. (2007). An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro. <em>Nucleic Acids Res.<\/em> <strong>35<\/strong>, 6042-6051.<\/p>\n<p>Gras, S., Chaumont, V., Fernandez, B., Carpentier, P., Charrier-Savournin, F., Schmitt, S., Pineau, C., Flament, D., <strong>Hecker, A.<\/strong>, Forterre, P., Armengaud, J. and Housset, D. (2007). Structural insights into a new homodimeric self-activated GTPase family. <em>EMBO Rep.<\/em> <strong>8<\/strong>, 569-575.<\/p>\n<p><strong>2005<\/strong><\/p>\n<p>Marin, F., Amons, R., Stigter, M., <strong>Hecker, A.<\/strong>, Luquet, G., Layrolle, P., Vicente, N., de Groot, K. and Westbroek, P. (2005). Caspartin and calprismin, two new proteins of the shell calcitic prisms of the Mediterranean fan mussel Pinna nobilis. <em>J. Biol. Chem.<\/em> <strong>280<\/strong>, 33895-33908.<\/p>\n<p><strong>2004<\/strong><\/p>\n<p>Luquet, G., <strong>Hecker, A.<\/strong> and Marin, F. (2004). Orchestin, a key calcium-binding phosphoprotein in the cyclic elaboration of two different ACC storage structures by the crustacean, Orchestia cavimana. Proceedings of the 8th ICCBMT, October 17-22, Banff Centre, Alberta, Canada, Landis W.L. &amp; Sodek J. Eds., pp. 111-114 (book chapter).<\/p>\n<p><strong>Hecker, A.<\/strong>, Quennedey, B., Testeni\u00e8re, O., Quennedey, A., Graf, F. and Luquet, G. (2004). Orchestin, a calcium-binding phosphoprotein is a matrix component of two successive transitory calcified biomineralizations elaborated cyclically by a terrestrial crustacean. <em>J. Struct. Biol.<\/em> <strong>146<\/strong>, 310-324.<\/p>\n<p><strong>2003<\/strong><\/p>\n<p><strong>Hecker, A.<\/strong>, Testeni\u00e8re, O., Marin, F. and Luquet, G. (2003). Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium storage structures. <em>FEBS Lett<\/em>. <strong>535<\/strong>, 49-54.<\/p>\n<p><strong>2002<\/strong><\/p>\n<p>Raz, S., Testeni\u00e8re, O., <strong>Hecker, A.<\/strong>, Weiner, S. and Luquet, G. (2002). Stable amorphous calcium carbonate is the main component of the calcium storage structures of a terrestrial crustacean. <em>Biol. Bull<\/em>., <strong>203<\/strong>, 269-274.<\/p>\n<p>Testeni\u00e8re, O., <strong>Hecker, A.<\/strong>, Le Gurun, S., Quennedey, B., Graf, F. and Luquet, G. (2002). Characterization and spatio-temporal expression of Orchestin, a gene encoding an ecdysone-inducible calcium binding protein from a crustacean organic matrix. <em>Biochem. J.<\/em> <strong>361<\/strong>, 327-335.<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Bio: I received\u00a0a Ph.D in Biology, Cellular and Molecular Biology\u00a0from the University of Burgundy (Dijon) in 2002. Under the supervision of Pr. Gilles Luquet, my research activities focused on the structure-function analysis\u00a0of Orchestin, a protein involved in a biomineralization process &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=110\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"parent":853,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-110","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/110","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=110"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/110\/revisions"}],"up":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/853"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=110"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}