{"id":9295,"date":"2018-10-22T13:29:01","date_gmt":"2018-10-22T13:29:01","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9295"},"modified":"2018-10-22T13:33:21","modified_gmt":"2018-10-22T13:33:21","slug":"9295","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9295","title":{"rendered":"Article: Antioxidants"},"content":{"rendered":"<p><a class=\"gsc_a_at\" href=\"http:\/\/scholar.google.fr\/scholar_url?url=http:\/\/www.mdpi.com\/2076-3921\/7\/10\/142\/pdf&amp;hl=fr&amp;sa=X&amp;d=11906918313259136293&amp;scisig=AAGBfm1MRAavToiy8OBjIoRgv5iIa_4ikA&amp;nossl=1&amp;oi=scholaralrt&amp;hist=a62_fy8AAAAJ:17538896607771456966:AAGBfm3NSCFdNcrOcWRdrFqfkwtsNk77pA\" data-href=\"\/citations?view_op=view_citation&amp;hl=fr&amp;user=u0KB0xMAAAAJ&amp;sortby=pubdate&amp;citation_for_view=u0KB0xMAAAAJ:ClCfbGk0d_YC\">Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron\u2013Sulfur Cluster and Reduce NFU Proteins In Vitro.\u00a0<\/a>F Zannini, T Roret, J Przybyla-Toscano, T Dhalleine, N Rouhier, &#8230;Antioxidants 7 (10), 14<\/p>\n<h1><span class=\"Apple-converted-space\">\u00a0<\/span>Abstract:<\/h1>\n<p style=\"text-align: justify;\">In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one\u00a0or two isoforms belonging to the TRX h or o classes, being less well developed compared to the\u00a0numerous isoforms found in chloroplasts. Unlike most other plant species, Arabidopsis thaliana\u00a0possesses two TRXo isoforms whose physiological functions remain unclear. Here, we performed a\u00a0structure\u2013function analysis to unravel the respective properties of the duplicated TRXo1 and TRXo2\u00a0isoforms. Surprisingly, when expressed in Escherichia coli, both recombinant proteins existed in\u00a0an apo-monomeric form and in a homodimeric iron\u2013sulfur (Fe-S) cluster-bridged form. In TRXo2,\u00a0the [4Fe-4S] cluster is likely ligated in by the usual catalytic cysteines present in the conserved\u00a0Trp-Cys-Gly-Pro-Cys signature. Solving the three-dimensional structure of both TRXo apo-forms\u00a0pointed to marked differences in the surface charge distribution, notably in some area usually\u00a0participating to protein\u2013protein interactions with partners. However, we could not detect a difference\u00a0in their capacity to reduce nitrogen-fixation-subunit-U (NFU)-like proteins, NFU4 or NFU5, two\u00a0proteins participating in the maturation of certain mitochondrial Fe-S proteins and previously isolated\u00a0as putative TRXo1 partners. Altogether, these results suggest that a novel regulation mechanism\u00a0may prevail for mitochondrial TRXs o, possibly existing as a redox-inactive Fe-S cluster-bound\u00a0form that could be rapidly converted in a redox-active form upon cluster degradation in specific\u00a0physiological conditions.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron\u2013Sulfur Cluster and Reduce NFU Proteins In Vitro.\u00a0F Zannini, T Roret, J Przybyla-Toscano, T Dhalleine, N Rouhier, &#8230;Antioxidants 7 (10), 14 \u00a0Abstract: In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one\u00a0or &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=9295\">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-9295","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\/9295","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=9295"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/9295\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=9295"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=9295"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=9295"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}