Metal-dependent glycosylation in recombinant metallothioneins. Issue 99 (23rd November 2022)

• Record Type: Journal Article
• Authors: García-Risco, Mario; González, Ana; Calatayud, Sara; Lopez-Jaramillo, Francisco J.; Pedrini-Martha, Veronika; Albalat, Ricard; Dallinger, Reinhard; Dominguez-Vera, José M.; Palacios, Òscar; Capdevila, Mercè
• Is Part Of: Chemical communications. Volume 58:Issue 99(2022)
• Page Start: 13755
• Page End: 13758
• Publication Date: 2022-11-23
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d2cc05589a
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Glycosylation of recombinant metalloproteins by means of Escherichia coli has been reported for the first time. This process is switched off by Cd 2+ ions and modulated by the proteins' metal-binding preference towards Zn 2+ or Cu + ions. Abstract : We show for the first time glycosylation of recombinant metallothioneins (MTs) produced in E. coli . Interestingly, our results show that the glycosylation level of the recombinant MTs is inversely proportional to the degree of protein structuration, and reflects their different metal preferences.