{"id":2164,"date":"2013-06-24T13:38:44","date_gmt":"2013-06-24T13:38:44","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=2164"},"modified":"2013-06-24T13:39:53","modified_gmt":"2013-06-24T13:39:53","slug":"anr-blanc-fes-traffic","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=2164","title":{"rendered":"ANR Blanc: FeS Traffic"},"content":{"rendered":"<h4><b>\u00a0<\/b>The project FeS Traffic coordinated by N. Rouhier has been selected by the ANR Blanc Committee<\/h4>\n<h4><\/h4>\n<h4><strong style=\"text-align: justify;\">Summary<\/strong><\/h4>\n<h4 style=\"text-align: justify;\">Several metabolic pathways and cellular processes in plants depend on the functioning of iron-sulfur (Fe-S) proteins, whose cofactor is assembled through dedicated assembly machineries. To cite only a few examples, Fe-S proteins are needed for photosynthesis, respiration, sulfur and nitrogen assimilation, co-enzyme synthesis and by similarity with other eukaryotes, for DNA repair and replication or ribosome biogenesis. In plants as in other organisms, the incorporation of Fe-S clusters into proteins requires first the <i>de novo<\/i> assembly of Fe-S clusters onto scaffold proteins and then the transfer of these pre-formed clusters to acceptor proteins via the action of several chaperones and\/or so-called carrier proteins. Using a combination of genetic, physiological, biochemical and structural approaches, the general objective of this research proposal is to understand precisely the molecular mechanisms controlling the second step, <i>i.e.,<\/i> the delivery of Fe-S clusters from scaffold proteins to final acceptors, in the context of the chloroplastic and mitochondrial Fe-S cluster assembly machineries. Whereas the majority of the proteins required to assemble Fe-S clusters in the cells have likely been identified, the <i>in vivo <\/i>roles of many components, essentially those involved in Fe-S cluster trafficking, remain to be clarified. Owing to the fact that there are several dozens of Fe-S proteins but relatively few scaffold proteins in cells, carrier proteins are essential sentinels ensuring the correct and specific distribution of the different types of Fe-S clusters to acceptor client proteins. This project focuses on the Nfu and A-type carrier protein families which are assumed, from current working models, to be the major contributors for the trafficking of Fe-S clusters. Incidentally, in addition to providing improved knowledge on the global functioning of these biogenesis systems, the designed experimental program, which combines <i>in vitro<\/i> <i>and in vivo<\/i> approaches, should bring crucial information about the cellular network and regulatory mechanisms coordinating the concerted action of the different components.<\/h4>\n<h4 style=\"text-align: justify;\"><\/h4>\n<h4 style=\"text-align: justify;\"><strong>R\u00e9sum\u00e9<\/strong><\/h4>\n<h4 style=\"text-align: justify;\">De nombreux processus cellulaires et voies m\u00e9taboliques d\u00e9pendent du fonctionnement de prot\u00e9ines fer-soufre (Fe-S), dont le cofacteur est assembl\u00e9 par des machineries d\u2019assemblage sp\u00e9cifiques. Pour ne citer que quelques exemples, les prot\u00e9ines Fe-S sont requises pour la photosynth\u00e8se, la respiration, l\u2019assimilation de l\u2019azote et du soufre ou la synth\u00e8se de co-enzymes mais \u00e9galement, par extension du travail r\u00e9alis\u00e9 chez d\u2019autres eucaryotes, pour la r\u00e9plication et la r\u00e9paration de l\u2019ADN et la synth\u00e8se des ribosomes. Chez les plantes, comme chez les autres organismes, l\u2019incorporation de centres Fe-S dans les prot\u00e9ines n\u00e9cessite l\u2019assemblage de novo des centres Fe-S sur des prot\u00e9ines d\u2019\u00e9chafaudage puis le transfert de ces centres pr\u00e9form\u00e9s aux prot\u00e9ines cibles. Ce transfert est effectu\u00e9 via l\u2019action de prot\u00e9ines chaperonnes et\/ou de prot\u00e9ines de transfert. En combinant des approches g\u00e9n\u00e9tiques, physiologiques, biochimiques et de biologie structurale, l\u2019objectif g\u00e9n\u00e9ral de ce projet de recherche est de comprendre pr\u00e9cis\u00e9ment les m\u00e9canismes mol\u00e9culaires qui contr\u00f4lent cette seconde \u00e9tape d\u2019\u00e9change de centres Fe-S au niveau des machineries chloroplastique et mitochondriale. En effet, alors que la plupart des prot\u00e9ines impliqu\u00e9es dans la biogen\u00e8se des centres fer-soufre ont probablement \u00e9t\u00e9 identifi\u00e9es, leur r\u00f4le exact, notamment celui des prot\u00e9ines participant aux \u00e9changes de centres\u00a0 Fe-S, reste \u00e0 \u00e9lucider. Etant donn\u00e9 qu\u2019il existe plusieurs douzaines de prot\u00e9ines Fe-S mais un nombre limit\u00e9 de prot\u00e9ines d\u2019\u00e9chafaudage, les prot\u00e9ines de transfert pourraient \u00eatre principalement n\u00e9cessaires pour la r\u00e9partition correcte et sp\u00e9cifique des diff\u00e9rents types de centres Fe-S aux prot\u00e9ines clientes. Ce projet se focalise sur deux familles de prot\u00e9ines, les prot\u00e9ines Nfu et les prot\u00e9ines de transfert de type A (ATC pour A-type carrier en anglais), qui repr\u00e9sentent vraisemblablement, d\u2019apr\u00e8s les mod\u00e8les actuels, les acteurs principaux r\u00e9gulant les \u00e9changes de centres Fe-S dans les cellules. Ce programme de recherche, combinant des approches in vitro et in vivo, va permettre d\u2019obtenir des informations pr\u00e9cieuses et originales sur le fonctionnement de ces syst\u00e8mes de biogen\u00e8se mais aussi sur les r\u00e9seaux d\u2019interaction et les m\u00e9canismes de r\u00e9gulation permettant de coordonner l\u2019action des diff\u00e9rentes prot\u00e9ines dans les cellules.<\/h4>\n","protected":false},"excerpt":{"rendered":"<p>\u00a0The project FeS Traffic coordinated by N. Rouhier has been selected by the ANR Blanc Committee Summary Several metabolic pathways and cellular processes in plants depend on the functioning of iron-sulfur (Fe-S) proteins, whose cofactor is assembled through dedicated assembly &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=2164\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[3],"tags":[],"class_list":["post-2164","post","type-post","status-publish","format-standard","hentry","category-internal-information"],"_links":{"self":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/2164","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/types\/post"}],"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=2164"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/2164\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=2164"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=2164"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=2164"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}