{"id":4198,"date":"2014-10-02T10:50:48","date_gmt":"2014-10-02T10:50:48","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=4198"},"modified":"2014-10-02T10:51:32","modified_gmt":"2014-10-02T10:51:32","slug":"article-biochimica-et-biophysica-acta","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=4198","title":{"rendered":"Article: Biochimica et Biophysica Acta"},"content":{"rendered":"<h5><a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S0167488914003437\">The roles of glutaredoxins ligating Fe-S clusters: Sensing, transfer or repair functions?<\/a><\/h5>\n<h5>J Couturier, J Przybyla-Toscano, T Roret, C Didierjean, N Rouhier<\/h5>\n<h5>Biochimica et Biophysica Acta (BBA)-Molecular Cell Research<\/h5>\n<h2><\/h2>\n<h2 id=\"authorab00051\">Abstract<\/h2>\n<p id=\"sp0005\" style=\"text-align: justify;\">Glutaredoxins (Grxs) are major oxidoreductases involved in the reduction of glutathionylated proteins. Owing to the capacity of several class I Grxs and likely all class II Grxs to incorporate iron\u2013sulfur (Fe\u2013S) clusters, they are also linked to iron metabolism. Most Grxs bind [2Fe\u20132S] clusters which are oxidatively- and reductively-labile and have identical ligation, involving notably external glutathione. However, subtle differences in the structural organization explain that class II Fe\u2013S Grxs, having more labile and solvent-exposed clusters, can accept Fe\u2013S clusters and transfer them to client proteins, whereas class I Fe\u2013S Grxs usually do not. From the observed glutathione disulfide-mediated Fe\u2013S cluster degradation, the current view is that the more stable Fe\u2013S clusters found in class I Fe\u2013S Grxs might constitute a sensor of oxidative stress conditions by modulating their activity. Indeed, in response to an oxidative signal, inactive holoforms i.e., without disulfide reductase activity, should be converted to active apoforms. Among class II Fe\u2013S Grxs, monodomain Grxs likely serve as carrier proteins for the delivery of preassembled Fe\u2013S clusters to acceptor proteins in organelles. Another proposed function is the repair of Fe\u2013S clusters. From their cytoplasmic and\/or nuclear localization, multidomain Grxs function in signalling pathways. In particular, they regulate iron homeostasis in yeast species by modulating the activity of transcription factors and eventually forming heterocomplexes with BolA-like proteins in response to the cellular iron status. We provide an overview of the biochemical and structural properties of Fe\u2013S cluster-loaded Grxs in relation to their hypothetical or confirmed associated functions. This article is part of a Special Issue entitled: Fe\/S proteins: Analysis, structure, function, biogenesis and diseases.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>The roles of glutaredoxins ligating Fe-S clusters: Sensing, transfer or repair functions? J Couturier, J Przybyla-Toscano, T Roret, C Didierjean, N Rouhier Biochimica et Biophysica Acta (BBA)-Molecular Cell Research Abstract Glutaredoxins (Grxs) are major oxidoreductases involved in the reduction of &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=4198\">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":[2],"tags":[],"class_list":["post-4198","post","type-post","status-publish","format-standard","hentry","category-academic-productions"],"_links":{"self":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/4198","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=4198"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/4198\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=4198"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=4198"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=4198"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}