<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Domenech, Jordi</style></author><author><style face="normal" font="default" size="100%">Mir, Gisela</style></author><author><style face="normal" font="default" size="100%">Huguet, Gemma</style></author><author><style face="normal" font="default" size="100%">Capdevila, Merce</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author><author><style face="normal" font="default" size="100%">Atrian, Silvia</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Plant metallothionein domains: functional insight into physiological metal binding and protein folding</style></title><secondary-title><style face="normal" font="default" size="100%">BIOCHIMIE</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cu-aggregates</style></keyword><keyword><style  face="normal" font="default" size="100%">metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">MT dimers</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus suber</style></keyword><keyword><style  face="normal" font="default" size="100%">separate Cys-rich domains</style></keyword><keyword><style  face="normal" font="default" size="100%">spacer region</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast complementation</style></keyword><keyword><style  face="normal" font="default" size="100%">Zn-aggregates</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><publisher><style face="normal" font="default" size="100%">ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER</style></publisher><pub-location><style face="normal" font="default" size="100%">23 RUE LINOIS, 75724 PARIS, FRANCE</style></pub-location><volume><style face="normal" font="default" size="100%">88</style></volume><pages><style face="normal" font="default" size="100%">583-593</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plant metallothioneins (MTs) differ from animal MTs by a peculiar sequence organization consisting of two short cysteine-rich terminal domains linked by a long cysteine-devoid spacer. The role of the plant NIT domains in the protein structure and functionality is largely unknown. Here, we investigate the separate domain contribution to the in vivo binding of Zn and Cu and to confer metal tolerance to CUP1-null yeast cells of a plant type 2 NIT (QsMT). For this purpose, we obtained three recombinant peptides that, respectively, correspond to the single N-terminal (N25) and C-terminal (C18) cysteine-rich domains of QsMT, and a chimera in which the spacer is replaced with a four-glycine bridge (N25-C18). The metal-peptide preparations recovered from Zn- or Cu-enriched cultures were characterized by ESI-MS, ICP-OES and CD and UV-vis spectroscopy and data compared to full length QsMT. Results are consistent with QsMT giving rise to homometallic Zn- or Cu-MT complexes according to a hairpin model in which the two Cys-rich domains interact to form a cluster. In this model the spacer region does not contribute to the metal coordination. However, our data from Zn-QsMT (but not from Cu-QsMT) support a fold of the spacer involving some interaction with the metal core. On the other hand, results from functional complementation assays in endogenous MT-defective yeast cells suggest that the spacer region may play a role in Cu-QsMT stability or subcellular localization. As a whole, our results provide the first insight into the structure/function relationship of plant MTs using the analysis of the separate domain abilities to bind physiological metals. (c) 2005 Elsevier SAS. All rights reserved.</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Domenech, Jordi</style></author><author><style face="normal" font="default" size="100%">Mir, Gisela</style></author><author><style face="normal" font="default" size="100%">Huguet, Gemma</style></author><author><style face="normal" font="default" size="100%">Capdevila, Merce</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author><author><style face="normal" font="default" size="100%">Atrian, Silvia</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Plant metallothionein domains: functional insight into physiological metal binding and protein folding</style></title><secondary-title><style face="normal" font="default" size="100%">BIOCHIMIE</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cu-aggregates</style></keyword><keyword><style  face="normal" font="default" size="100%">metallothionein</style></keyword><keyword><style  face="normal" font="default" size="100%">MT dimers</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus suber</style></keyword><keyword><style  face="normal" font="default" size="100%">separate Cys-rich domains</style></keyword><keyword><style  face="normal" font="default" size="100%">spacer region</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast complementation</style></keyword><keyword><style  face="normal" font="default" size="100%">Zn-aggregates</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006///</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">88</style></volume><pages><style face="normal" font="default" size="100%">583 - 593</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plant metallothioneins (MTs) differ from animal MTs by a peculiar sequence organization consisting of two short cysteine-rich terminal domains linked by a long cysteine-devoid spacer. The role of the plant NIT domains in the protein structure and functionality is largely unknown. Here, we investigate the separate domain contribution to the in vivo binding of Zn and Cu and to confer metal tolerance to CUP1-null yeast cells of a plant type 2 NIT (QsMT). For this purpose, we obtained three recombinant peptides that, respectively, correspond to the single N-terminal (N25) and C-terminal (C18) cysteine-rich domains of QsMT, and a chimera in which the spacer is replaced with a four-glycine bridge (N25-C18). The metal-peptide preparations recovered from Zn- or Cu-enriched cultures were characterized by ESI-MS, ICP-OES and CD and UV-vis spectroscopy and data compared to full length QsMT. Results are consistent with QsMT giving rise to homometallic Zn- or Cu-MT complexes according to a hairpin model in which the two Cys-rich domains interact to form a cluster. In this model the spacer region does not contribute to the metal coordination. However, our data from Zn-QsMT (but not from Cu-QsMT) support a fold of the spacer involving some interaction with the metal core. On the other hand, results from functional complementation assays in endogenous MT-defective yeast cells suggest that the spacer region may play a role in Cu-QsMT stability or subcellular localization. As a whole, our results provide the first insight into the structure/function relationship of plant MTs using the analysis of the separate domain abilities to bind physiological metals. (c) 2005 Elsevier SAS. All rights reserved.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><notes><style face="normal" font="default" size="100%">The following values have no corresponding Zotero field:&lt;br/&gt;pub-location: 23 RUE LINOIS, 75724 PARIS, FRANCE&lt;br/&gt;publisher: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pla, Maria</style></author><author><style face="normal" font="default" size="100%">Huguet, Gemma</style></author><author><style face="normal" font="default" size="100%">Verdaguer, Dolors</style></author><author><style face="normal" font="default" size="100%">Puigderrajols, Pere</style></author><author><style face="normal" font="default" size="100%">Llompart, Blanca</style></author><author><style face="normal" font="default" size="100%">Nadal, Anna</style></author><author><style face="normal" font="default" size="100%">Molinas, Marisa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stress proteins co-expressed in suberized and lignified cells and in apical meristems</style></title><secondary-title><style face="normal" font="default" size="100%">Plant Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cork-oak</style></keyword><keyword><style  face="normal" font="default" size="100%">osmotin like proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">phellem</style></keyword><keyword><style  face="normal" font="default" size="100%">Quercus suber</style></keyword><keyword><style  face="normal" font="default" size="100%">small heat shock proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">tissue specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year></dates><volume><style face="normal" font="default" size="100%">139</style></volume><pages><style face="normal" font="default" size="100%">49-57</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We report the cloning of a small heat shock protein, Qs –HSP17, and an osmotin like protein, Qs –OLP, from cork oak phellem tissue (cork cells). Both genes are expressed in suberizing cells and in other cells subject to endogenous stress associated with free radicals. We provide evidence that smHSPs and OLPs accumulate in overwintering buds and speculate that their role is similar to that in seed dormancy. We also show that both stress proteins are mainly located in the region of the quiescent center in root apex and in central meristem in the shoot apex. We emphasize that smHSPs and OLPs are expressed in cells growing under endogenous stress or facing long life-span. We discuss a possible role of these stress proteins against oxidative stress</style></abstract></record></records></xml>