{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T02:38:39Z","timestamp":1788403119544,"version":"build-2803163510"},"reference-count":40,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2005,10,1]]},"abstract":"<jats:p>In previous studies, we showed that the chemical and dynamic properties of fish and mouse MTs (metallothioneins) present a number of distinctive differences linked to their primary structures, and that phylogenetic relationships of mammal and fish MTs correlate with their three-dimensional structures. The different behaviours of MTs may also be linked to the interaction between their two domains. In the present study, we have compared the physicochemical properties of the isolated recombinant domains constituting Notothenia coriiceps and mouse MTs, and compared them with those of the corresponding whole MTs. NMR spectra of the separated domains of N. coriiceps are almost superimposable on those of the parent MT, suggesting an apparent lack of interaction between the two domains in the protein. However, certain dynamic and physicochemical features of the isolated domains are unlike those of the whole protein. In particular, the temperature-induced changes in the chiroptical properties, thiol reactivity of the Zn-MT domains and the Zn2+\/Cd2+ rate of exchange are different for the two domains and with respect to the whole protein. Taken together, these results provide a strong argument in favour of the interaction of the two domains in the MT molecule, in spite of the elusive evidence provided by the structural analyses.<\/jats:p>","DOI":"10.1042\/bj20050335","type":"journal-article","created":{"date-parts":[[2005,9,26]],"date-time":"2005-09-26T14:46:34Z","timestamp":1127745994000},"page":"95-103","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Structural and functional studies of vertebrate metallothioneins: cross-talk between domains in the absence of physical contact"],"prefix":"10.1042","volume":"391","author":[{"given":"Clemente","family":"Capasso","sequence":"first","affiliation":[{"name":"CNR, Institute of Protein Biochemistry, via P. Castellino 111 I 80131 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincenzo","family":"Carginale","sequence":"additional","affiliation":[{"name":"CNR, Institute of Protein Biochemistry, via P. Castellino 111 I 80131 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Orlando","family":"Crescenzi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Naples \u201cFederico II\u201d, via Cinthia 45 I 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"Di\u00a0Maro","sequence":"additional","affiliation":[{"name":"BIOMODEM (Biomolecular Demonstrations) PSCRL (Piccola Societ\u00e0 Cooperativa a Responsabilit\u00e0 Limitata), via Fiorentina I 53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta","family":"Spadaccini","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Naples \u201cFederico II\u201d, via Cinthia 45 I 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Piero\u00a0Andrea","family":"Temussi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Naples \u201cFederico II\u201d, via Cinthia 45 I 80126 Naples, Italy"},{"name":"National Institute for Medical Research, Medical Research Council, The Ridgeway, Mill Hill, London NW7 1AA, U.K."},{"name":"Centro Linceo \u201cBeniamino Segre\u201d, Accademia dei Lincei, Via della Lungara, 10 I 00165 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elio","family":"Parisi","sequence":"additional","affiliation":[{"name":"CNR, Institute of Protein Biochemistry, via P. Castellino 111 I 80131 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2005,9,26]]},"reference":[{"key":"2021112217140832400_B1","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0753-3322(03)00081-7","article-title":"Trace elements in human physiology and pathology: zinc and metallothioneins","volume":"57","author":"Tapiero","year":"2003","journal-title":"Biomed. Pharmacother."},{"key":"2021112217140832400_B2","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1042\/bst0300766","article-title":"Responses of plants to iron, zinc and copper deficiencies","volume":"30","author":"Wintz","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"2021112217140832400_B3","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/S1471-4892(03)00115-2","article-title":"Targeting metalloenzymes: a strategy that works","volume":"3","author":"White","year":"2003","journal-title":"Curr. Opin. Pharmacol."},{"key":"2021112217140832400_B4","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0027-5107(01)00067-7","article-title":"Zinc and the gene","volume":"475","author":"Dreosti","year":"2001","journal-title":"Mutat. Res."},{"key":"2021112217140832400_B5","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1093\/bfgp\/1.4.342","article-title":"Recent developments in the engineering of zinc finger proteins","volume":"1","author":"Moore","year":"2003","journal-title":"Brief. Funct. Genomic. Proteomic."},{"key":"2021112217140832400_B6","first-page":"28","article-title":"Metallothioneins: the structure and mechanisms of action","volume":"75","author":"Baraboi","year":"2003","journal-title":"Ukr. Biokhim. Zh."},{"key":"2021112217140832400_B7","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1007\/s00018-002-8454-2","article-title":"Metallothionein: the multipurpose protein","volume":"59","author":"Coyle","year":"2002","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112217140832400_B8","doi-asserted-by":"crossref","first-page":"1455S","DOI":"10.1093\/jn\/130.5.1455S","article-title":"The function of zinc metallothionein: a link between cellular zinc and redox state","volume":"130","author":"Maret","year":"2000","journal-title":"J. Nutr."},{"key":"2021112217140832400_B9","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S1367-5931(00)00082-X","article-title":"Metallothioneins: new functional and structural insights","volume":"4","author":"Vasak","year":"2000","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2021112217140832400_B10","first-page":"223","article-title":"Metallothionein: an exceptional metal thiolate protein","volume":"72","author":"Kagi","year":"1979","journal-title":"Ciba Found. Symp."},{"key":"2021112217140832400_B11","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S0021-9258(18)48484-0","article-title":"Studies on the assembly and stability of the metalthiolate clusters of metallothionein in dimethyl sulfoxide","volume":"267","author":"Rakshit","year":"1992","journal-title":"J. Biol. Chem."},{"key":"2021112217140832400_B12","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1002\/prot.10050","article-title":"Stability and conformational dynamics of metallothioneins from the Antarctic fish Notothenia coriiceps and mouse","volume":"46","author":"Capasso","year":"2002","journal-title":"Proteins"},{"key":"2021112217140832400_B13","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/978-3-0348-6784-9_18","article-title":"Cadmium binding and metal cluster formation in metallothionein: a differential modification study","volume":"52","author":"Bernhard","year":"1987","journal-title":"Experientia Suppl."},{"key":"2021112217140832400_B14","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.1073\/pnas.97.6.2503","article-title":"Zinc transfer potentials of the \u03b1- and \u03b2-clusters of metallothionein are affected by domain interactions in the whole molecule","volume":"97","author":"Jiang","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112217140832400_B15","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.bbrc.2004.03.183","article-title":"Cu+ distribution in metallothionein fragments","volume":"318","author":"Salgado","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021112217140832400_B16","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1073\/pnas.95.7.3489","article-title":"Control of zinc transfer between thionein, metallothionein, and zinc proteins","volume":"95","author":"Jacob","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112217140832400_B17","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0197-0186(95)00114-X","article-title":"Role of metallothionein and other antioxidants in scavenging superoxide radicals and their possible role in neuroprotection","volume":"29","author":"Hussain","year":"1996","journal-title":"Neurochem. Int."},{"key":"2021112217140832400_B18","doi-asserted-by":"crossref","first-page":"1460S","DOI":"10.1093\/jn\/133.5.1460S","article-title":"Cellular zinc and redox states converge in the metallothionein\/thionein pair","volume":"133","author":"Maret","year":"2003","journal-title":"J. Nutr."},{"key":"2021112217140832400_B19","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1016\/j.jinorgbio.2004.02.005","article-title":"Metallothionein can function as a chaperone for zinc uptake transport into prostate and liver mitochondria","volume":"98","author":"Costello","year":"2004","journal-title":"J. Inorg. Biochem."},{"key":"2021112217140832400_B20","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/978-3-0348-6784-9_3","article-title":"Chemistry and biochemistry of metallothionein","volume":"52","author":"Kagi","year":"1987","journal-title":"Experientia Suppl."},{"key":"2021112217140832400_B21","first-page":"331","article-title":"Metallothioneins in terrestrial invertebrates: structural aspects, biological significance and implications for their use as biomarkers","volume":"46","author":"Dallinger","year":"2000","journal-title":"Cell. Mol. Biol. (Paris)"},{"key":"2021112217140832400_B22","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/40785","article-title":"Metallothionein in snail Cd and Cu metabolism","volume":"388","author":"Dallinger","year":"1997","journal-title":"Nature (London)"},{"key":"2021112217140832400_B23","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1042\/bj3540291","article-title":"Structural characterization and thermal stability of Notothenia coriiceps metallothionein","volume":"354","author":"D'Auria","year":"2001","journal-title":"Biochem. J."},{"key":"2021112217140832400_B24","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S0969-2126(03)00044-3","article-title":"Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps","volume":"11","author":"Capasso","year":"2003","journal-title":"Structure (Camb.)"},{"key":"2021112217140832400_B25","doi-asserted-by":"crossref","first-page":"S250","DOI":"10.1007\/s00239-003-0034-z","article-title":"Phylogenetic divergence of fish and mammalian metallothionein: relationships with structural diversification and organismal temperature","volume":"57","author":"Capasso","year":"2003","journal-title":"J. Mol. Evol."},{"key":"2021112217140832400_B26","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1093\/oxfordjournals.jbchem.a021701","article-title":"Purification and characteristics of recombinant mouse metallothionein-I from Escherichia coli","volume":"121","author":"Xiong","year":"1997","journal-title":"J. Biochem. (Tokyo)"},{"key":"2021112217140832400_B27","first-page":"104","article-title":"DNA sequencing with chain-terminating inhibitors [1977]","volume":"24","author":"Sanger","year":"1992","journal-title":"Biotechnology"},{"key":"2021112217140832400_B28","doi-asserted-by":"crossref","first-page":"3478","DOI":"10.1073\/pnas.95.7.3478","article-title":"Thiolate ligands in metallothionein confer redox activity on zinc clusters","volume":"95","author":"Maret","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112217140832400_B29","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"2021112217140832400_B30","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1007\/BF00404272","article-title":"NMRView: A computer program for the visualization and analysis of NMR data","volume":"4","author":"Johnson","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"2021112217140832400_B31","doi-asserted-by":"crossref","first-page":"2229","DOI":"10.1063\/1.432450","article-title":"NMRView: A computer program for the visualization and analysis of NMR data","volume":"64","author":"Aue","year":"1976","journal-title":"J. Chem. Phys."},{"key":"2021112217140832400_B32","first-page":"355","article-title":"MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy","volume":"65","author":"Bax","year":"1985","journal-title":"J. Magn. Reson."},{"key":"2021112217140832400_B33","doi-asserted-by":"crossref","first-page":"4546","DOI":"10.1063\/1.438208","article-title":"Investigation of exchange process by two-dimensional NMR spectroscopy","volume":"71","author":"Jeener","year":"1979","journal-title":"J. Chem. Phys."},{"key":"2021112217140832400_B34","doi-asserted-by":"crossref","DOI":"10.1051\/epn\/19861701011","article-title":"NMR of proteins and nucleic acids","author":"W\u00fcthrich","year":"1986"},{"key":"2021112217140832400_B35","first-page":"670","article-title":"Suppression of Cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence","volume":"96","author":"Cavanagh","year":"1992","journal-title":"J. Magn. Reson."},{"key":"2021112217140832400_B36","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/0006-291X(83)91093-8","article-title":"Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins","volume":"113","author":"Marion","year":"1983","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021112217140832400_B37","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1007\/BF02192855","article-title":"Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions","volume":"2","author":"Piotto","year":"1992","journal-title":"J. Biomol. NMR"},{"key":"2021112217140832400_B38","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.gene.2004.11.024","article-title":"Fish and mammalian metallothioneins: a comparative study","volume":"345","author":"Scudiero","year":"2005","journal-title":"Gene"},{"key":"2021112217140832400_B39","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1110\/ps.04804504","article-title":"Prediction of pKa and redox properties in the thioredoxin superfamily","volume":"13","author":"Moutevelis","year":"2004","journal-title":"Protein Sci."},{"key":"2021112217140832400_B40","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/bj2110109","article-title":"Sea urchin (Anthocidaris crassispina) egg zinc-binding protein: cellular localization, purification and characterization","volume":"211","author":"Ohtake","year":"1983","journal-title":"Biochem. J."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/391\/1\/95\/638929\/bj3910095.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/391\/1\/95\/638929\/bj3910095.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T00:29:52Z","timestamp":1637627392000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/391\/1\/95\/78772\/Structural-and-functional-studies-of-vertebrate"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,9,26]]},"references-count":40,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2005,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20050335","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2005,9,26]]}}}