Structural characterization and thermal stability of Notothenia coriiceps metallothionein
Fish and mammalian metallothioneins (MTs) differ in the amino acid residues placed between their conserved cysteines. We have expressed the MT of an Antarctic fish, Notothenia coriiceps, and characterized it by means of multinuclear NMR spectroscopy. Overall, the architecture of the fish MT is very...
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ftunivnapoliiris:oai:www.iris.unina.it:11588/641317 2024-06-23T07:46:39+00:00 Structural characterization and thermal stability of Notothenia coriiceps metallothionein D'Auria, S. Carginale, V. Di Maro, D. Parisi, E. Capasso, C. SCUDIERO, ROSARIA CRESCENZI, ORLANDO TEMUSSI, PIERO ANDREA D'Auria, S. Carginale, V. Scudiero, Rosaria Crescenzi, Orlando Di Maro, D. Temussi, PIERO ANDREA Parisi, E. Capasso, C. 2001 http://hdl.handle.net/11588/641317 https://doi.org/10.1042/0264-6021:3540291 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000167483700008 volume:354 issue:2 firstpage:291 lastpage:299 numberofpages:9 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/11588/641317 doi:10.1042/0264-6021:3540291 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0035282063 Absorbance spectroscopy Circular dichroism NMR Temperature effect Zinc mobility Biochemistry info:eu-repo/semantics/article 2001 ftunivnapoliiris https://doi.org/10.1042/0264-6021:3540291 2024-06-10T14:58:50Z Fish and mammalian metallothioneins (MTs) differ in the amino acid residues placed between their conserved cysteines. We have expressed the MT of an Antarctic fish, Notothenia coriiceps, and characterized it by means of multinuclear NMR spectroscopy. Overall, the architecture of the fish MT is very similar to that of mammalian MTs. However, NMR spectroscopy shows that the dynamic behaviour of the two domains is markedly different. With the aid of absorption and CD spectroscopies, we studied the conformational and electronic features of fish and mouse recombinant Cd-MT and the changes produced in these proteins by heating. When the temperature was increased from 20 to 90 °C, the Cd-thiolate chromophore absorbance at 254 nm of mouse MT was not modified up to 60 °C, whereas the absorbance of fish MT decreased significantly starting from 30 °C. The CD spectra also changed quite considerably with temperature, with a gradual decrease of the positive band at 260 nm that was more pronounced for fish than for mouse MT. The differential effect of temperature on fish and mouse MTs may reflect a different stability of metal-thiolate clusters of the two proteins. Such a conclusion is also corroborated by results showing differences in metal mobility between fish and mouse Zn-MT. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
Absorbance spectroscopy Circular dichroism NMR Temperature effect Zinc mobility Biochemistry |
spellingShingle |
Absorbance spectroscopy Circular dichroism NMR Temperature effect Zinc mobility Biochemistry D'Auria, S. Carginale, V. Di Maro, D. Parisi, E. Capasso, C. SCUDIERO, ROSARIA CRESCENZI, ORLANDO TEMUSSI, PIERO ANDREA Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
topic_facet |
Absorbance spectroscopy Circular dichroism NMR Temperature effect Zinc mobility Biochemistry |
description |
Fish and mammalian metallothioneins (MTs) differ in the amino acid residues placed between their conserved cysteines. We have expressed the MT of an Antarctic fish, Notothenia coriiceps, and characterized it by means of multinuclear NMR spectroscopy. Overall, the architecture of the fish MT is very similar to that of mammalian MTs. However, NMR spectroscopy shows that the dynamic behaviour of the two domains is markedly different. With the aid of absorption and CD spectroscopies, we studied the conformational and electronic features of fish and mouse recombinant Cd-MT and the changes produced in these proteins by heating. When the temperature was increased from 20 to 90 °C, the Cd-thiolate chromophore absorbance at 254 nm of mouse MT was not modified up to 60 °C, whereas the absorbance of fish MT decreased significantly starting from 30 °C. The CD spectra also changed quite considerably with temperature, with a gradual decrease of the positive band at 260 nm that was more pronounced for fish than for mouse MT. The differential effect of temperature on fish and mouse MTs may reflect a different stability of metal-thiolate clusters of the two proteins. Such a conclusion is also corroborated by results showing differences in metal mobility between fish and mouse Zn-MT. |
author2 |
D'Auria, S. Carginale, V. Scudiero, Rosaria Crescenzi, Orlando Di Maro, D. Temussi, PIERO ANDREA Parisi, E. Capasso, C. |
format |
Article in Journal/Newspaper |
author |
D'Auria, S. Carginale, V. Di Maro, D. Parisi, E. Capasso, C. SCUDIERO, ROSARIA CRESCENZI, ORLANDO TEMUSSI, PIERO ANDREA |
author_facet |
D'Auria, S. Carginale, V. Di Maro, D. Parisi, E. Capasso, C. SCUDIERO, ROSARIA CRESCENZI, ORLANDO TEMUSSI, PIERO ANDREA |
author_sort |
D'Auria, S. |
title |
Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
title_short |
Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
title_full |
Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
title_fullStr |
Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
title_full_unstemmed |
Structural characterization and thermal stability of Notothenia coriiceps metallothionein |
title_sort |
structural characterization and thermal stability of notothenia coriiceps metallothionein |
publishDate |
2001 |
url |
http://hdl.handle.net/11588/641317 https://doi.org/10.1042/0264-6021:3540291 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000167483700008 volume:354 issue:2 firstpage:291 lastpage:299 numberofpages:9 journal:BIOCHEMICAL JOURNAL http://hdl.handle.net/11588/641317 doi:10.1042/0264-6021:3540291 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0035282063 |
op_doi |
https://doi.org/10.1042/0264-6021:3540291 |
_version_ |
1802647270329417728 |