{"id":9368,"date":"2018-12-04T07:03:40","date_gmt":"2018-12-04T07:03:40","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9368"},"modified":"2018-12-04T07:03:50","modified_gmt":"2018-12-04T07:03:50","slug":"article-biochimica-et-biophysica-acta-4","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9368","title":{"rendered":"Article: Biochimica et Biophysica Acta"},"content":{"rendered":"<p style=\"text-align: justify;\"><a class=\"gsc_a_at\" href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0304416518303635\" data-href=\"\/citations?view_op=view_citation&amp;hl=fr&amp;user=u0KB0xMAAAAJ&amp;sortby=pubdate&amp;citation_for_view=u0KB0xMAAAAJ:86PQX7AUzd4C\">The thioredoxin-mediated recycling of Arabidopsis thaliana GRXS16 relies on a conserved C-terminal cysteine\u00a0<\/a>F Zannini, A Moseler, R Bchini, T Dhalleine, AJ Meyer, N Rouhier, &#8230; Biochimica et Biophysica Acta (BBA)-General Subjects<\/p>\n<h2 class=\"section-title\" style=\"text-align: justify;\">Abstract<\/h2>\n<div id=\"as0005\" style=\"text-align: justify;\">\n<h3 id=\"st0010\">Background<\/h3>\n<p id=\"sp0100\">Glutaredoxins (GRXs) are oxidoreductases involved in diverse cellular processes through their capacity to reduce glutathionylated proteins and\/or to coordinate iron\u2011sulfur (Fe<img decoding=\"async\" src=\"https:\/\/sdfestaticassets-eu-west-1.sciencedirectassets.com\/shared-assets\/16\/entities\/sbnd\" alt=\"\" \/>S) clusters. Among class II GRXs, the plant-specific GRXS16 is a bimodular protein formed by an N-terminal endonuclease domain fused to a GRX domain containing a <sup>158<\/sup>CGFS signature.<\/p>\n<\/div>\n<div id=\"as0010\" style=\"text-align: justify;\">\n<h3 id=\"st0015\">Methods<\/h3>\n<p id=\"sp0105\">The biochemical properties (redox activity, sensitivity to oxidation, p<em>K<\/em><sub><em>a<\/em><\/sub> of cysteine residues, midpoint redox potential) of <em>Arabidopsis thaliana<\/em> GRXS16 were investigated by coupling oxidative treatments to alkylation shift assays, activity measurements and mass spectrometry analyses.<\/p>\n<\/div>\n<div id=\"as0015\" style=\"text-align: justify;\">\n<h3 id=\"st0020\">Results<\/h3>\n<p id=\"sp0110\">Activity measurements using redox-sensitive GFP2 (roGFP2) did not reveal any significant glutathione-dependent reductase activity of <em>A. thaliana<\/em> GRXS16 whereas it was able to catalyze its oxidation in the presence of glutathione disulfide. Accordingly, Arabidopsis GRXS16 reacted efficiently with oxidized forms of glutathione, leading to the formation of an intramolecular disulfide between Cys<sup>158<\/sup> and the semi-conserved Cys<sup>215<\/sup>, which has a midpoint redox potential of &#8211; 298\u202fmV at pH\u202f7.0 and is reduced by plastidial thioredoxins (TRXs) but not GSH. By promoting the formation of this disulfide, Cys<sup>215<\/sup> modulates GRXS16 oxidoreductase activity.<\/p>\n<\/div>\n<div id=\"as0020\" style=\"text-align: justify;\">\n<h3 id=\"st0025\">Conclusion<\/h3>\n<p id=\"sp0115\">The reduction of AtGRXS16, which is mandatory for its oxidoreductase activity and the binding of Fe<img decoding=\"async\" src=\"https:\/\/sdfestaticassets-eu-west-1.sciencedirectassets.com\/shared-assets\/16\/entities\/sbnd\" alt=\"\" \/>S clusters, depends on light through the plastidial FTR\/TRX system. Hence, disulfide formation may constitute a redox switch mechanism controlling GRXS16 function in response to day\/night transition or oxidizing conditions.<\/p>\n<\/div>\n<div id=\"as0025\">\n<h3 id=\"st0030\" style=\"text-align: justify;\">General significance.<\/h3>\n<p id=\"sp0120\" style=\"text-align: justify;\">From the <em>in vitro<\/em> data obtained with roGFP2, one can postulate that GRXS16 would mediate protein glutathionylation\/oxidation in plastids but not their deglutathionylation.<\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>The thioredoxin-mediated recycling of Arabidopsis thaliana GRXS16 relies on a conserved C-terminal cysteine\u00a0F Zannini, A Moseler, R Bchini, T Dhalleine, AJ Meyer, N Rouhier, &#8230; Biochimica et Biophysica Acta (BBA)-General Subjects Abstract Background Glutaredoxins (GRXs) are oxidoreductases involved in diverse &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9368\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[2],"tags":[],"class_list":["post-9368","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\/9368","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=9368"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/9368\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=9368"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=9368"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=9368"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}