{"id":3914,"date":"2014-07-15T06:24:14","date_gmt":"2014-07-15T06:24:14","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=3914"},"modified":"2014-07-15T06:24:14","modified_gmt":"2014-07-15T06:24:14","slug":"article-journal-of-biological-chemistry-2","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=3914","title":{"rendered":"Article: Journal of Biological Chemistry"},"content":{"rendered":"<p><a href=\"http:\/\/www.jbc.org\/content\/early\/2014\/07\/10\/jbc.M114.572701.short\">Structural and spectroscopic insights into BolA-glutaredoxin complexes<\/a><br \/>\nT Roret, P Tsan, J Couturier, B Zhang, MK Johnson, N Rouhier, &#8230;<br \/>\nJournal of Biological Chemistry, jbc. M114. 572701<\/p>\n<h2>Abstract<\/h2>\n<p id=\"p-5\" style=\"text-align: justify;\">BolA proteins are defined as stress-responsive transcriptional regulators but they also participate to iron metabolism. Although they can form [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking. Three Arabidopsis thaliana BolA structures were solved. They differ primarily by the size of a loop referred to as the variable [H\/C] loop which contains an important cysteine (BolA_C group) or histidine (BolA_H group) residue. From 3D modeling and spectroscopic analyses of A. thaliana GrxS14-BolA1 holo-heterodimer (BolA_H), we provide evidence for the coordination of a Rieske-type [2Fe-2S] cluster. For BolA_C members, the cysteine could replace the histidine as a ligand. NMR interaction experiments using apo-proteins indicate that a completely different heterodimer was formed, involving the nucleic acid binding site of BolA and the C-terminal tail of Grx. The possible biological importance of these complexes is discussed considering the physiological functions previously assigned to BolA and to Grx-BolA or Grx-Grx complexes.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Structural and spectroscopic insights into BolA-glutaredoxin complexes T Roret, P Tsan, J Couturier, B Zhang, MK Johnson, N Rouhier, &#8230; Journal of Biological Chemistry, jbc. M114. 572701 Abstract BolA proteins are defined as stress-responsive transcriptional regulators but they also participate &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=3914\">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-3914","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\/3914","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=3914"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/3914\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=3914"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=3914"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=3914"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}