{"id":8089,"date":"2017-04-06T19:11:28","date_gmt":"2017-04-06T19:11:28","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=8089"},"modified":"2017-04-06T19:12:04","modified_gmt":"2017-04-06T19:12:04","slug":"8089","status":"publish","type":"post","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=8089","title":{"rendered":"Article: PloS one"},"content":{"rendered":"<p><a class=\"gsc_a_at\" href=\"http:\/\/journals.plos.org\/plosone\/article?id=10.1371\/journal.pone.0174753\">Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A<\/a>\u00a0B Selles, F Zannini, J Couturier, JP Jacquot, N Rouhier\u00a0PloS one 12 (3), e0174753<\/p>\n<h2>Abstract<\/h2>\n<p style=\"text-align: justify;\">Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms. PDI-A is characterized by a single catalytic Trx module, the so-called\u00a0<em>a<\/em>\u00a0domain, whereas PDI-L1a and PDI-M display an\u00a0<em>a-b-b\u2019-a<\/em>\u2019 and\u00a0<em>a\u00b0-a-b<\/em>\u00a0organisation respectively. Their activities have been tested\u00a0<em>in vitro<\/em>\u00a0using purified recombinant proteins and a series of model substrates as insulin, NADPH thioredoxin reductase, NADP malate dehydrogenase (NADP-MDH), peroxiredoxins or RNase A. We demonstrated that PDI-A exhibited none of the usually reported activities, although the cysteines of the WCKHC active site signature are able to form a disulfide with a redox midpoint potential of -170 mV at pH 7.0. The fact that it is able to bind a [Fe2S2] cluster upon\u00a0<em>Escherichia coli<\/em>\u00a0expression and anaerobic purification might indicate that it does not have a function in dithiol-disulfide exchange reactions. The two other proteins were able to catalyze oxidation or reduction reactions, PDI-L1a being more efficient in most cases, except that it was unable to activate the non-physiological substrate NADP-MDH, in contrast to PDI-M. To further evaluate the contribution of the catalytic domains of PDI-M, the dicysteinic motifs have been independently mutated in each\u00a0<em>a<\/em>\u00a0domain. The results indicated that the two\u00a0<em>a<\/em>\u00a0domains seem interconnected and that the\u00a0<em>a\u00b0<\/em>\u00a0module preferentially catalyzed oxidation reactions whereas the\u00a0<em>a<\/em>\u00a0module catalyzed reduction reactions, in line with the respective redox potentials of -170 mV and -190 mV at pH 7.0. Overall, these\u00a0<em>in vitro<\/em>\u00a0results illustrate that the number and position of\u00a0<em>a<\/em>and\u00a0<em>b<\/em>\u00a0domains influence the redox properties and substrate recognition (both electron donors and acceptors) of PDI which contributes to understand why this protein family expanded along evolution.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A\u00a0B Selles, F Zannini, J Couturier, JP Jacquot, N Rouhier\u00a0PloS one 12 (3), e0174753 Abstract Protein disulfide isomerases are overwhelmingly multi-modular redox &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?p=8089\">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-8089","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\/8089","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=8089"}],"version-history":[{"count":0,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/posts\/8089\/revisions"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=8089"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=8089"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=8089"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}