Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones

Abstract This work analyzes the involvement of arginines in copper/H2O2-induced DNA breakage. Copper is a highly redox active metal which has been demonstrated to form compounds with arginines. For this aim we used mixtures of pGEM3 DNA plasmid and two types of H1 histones which differ only in their...

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Autores principales:	Marina Piscopo, Marco Trifuoggi, Carmela Scarano, Carla Gori, Antonella Giarra, Ferdinando Febbraio
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fc102ad6da5641df870dfccbaeeaf859
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spelling	oai:doaj.org-article:fc102ad6da5641df870dfccbaeeaf8592021-12-02T15:08:55ZRelevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones10.1038/s41598-018-25784-z2045-2322https://doaj.org/article/fc102ad6da5641df870dfccbaeeaf8592018-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25784-zhttps://doaj.org/toc/2045-2322Abstract This work analyzes the involvement of arginines in copper/H2O2-induced DNA breakage. Copper is a highly redox active metal which has been demonstrated to form compounds with arginines. For this aim we used mixtures of pGEM3 DNA plasmid and two types of H1 histones which differ only in their arginine content. The sperm H1 histone from the annelid worm Chaetopterus variopedatus (arginine content 12.6 mol% K/R ratio 2) and the somatic H1 histone from calf thymus (arginine content 1.8 mol% and K/R ratio 15). Copper/H2O2-induced DNA breakage was observed only in presence of sperm H1 histones, but it was more relevant for the native molecule than for the deguanidinated derivative (K/R ratio 14), in which 80% of arginine residues were converted to ornithine. Further, copper induced proteinase K resistance and increase of DNA binding affinity on native sperm H1 histones. These observations are consistent with a copper induced reorganization of the side-chains of arginine residues. Copper, instead, did not affect DNA binding affinity of somatic and deguanidinated H1 histones, which show similar K/R ratio and DNA binding mode. These results indicate that arginine residues could affect these H1 histones properties and provide new insights into copper toxicity mechanisms.Marina PiscopoMarco TrifuoggiCarmela ScaranoCarla GoriAntonella GiarraFerdinando FebbraioNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marina Piscopo Marco Trifuoggi Carmela Scarano Carla Gori Antonella Giarra Ferdinando Febbraio Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
description	Abstract This work analyzes the involvement of arginines in copper/H2O2-induced DNA breakage. Copper is a highly redox active metal which has been demonstrated to form compounds with arginines. For this aim we used mixtures of pGEM3 DNA plasmid and two types of H1 histones which differ only in their arginine content. The sperm H1 histone from the annelid worm Chaetopterus variopedatus (arginine content 12.6 mol% K/R ratio 2) and the somatic H1 histone from calf thymus (arginine content 1.8 mol% and K/R ratio 15). Copper/H2O2-induced DNA breakage was observed only in presence of sperm H1 histones, but it was more relevant for the native molecule than for the deguanidinated derivative (K/R ratio 14), in which 80% of arginine residues were converted to ornithine. Further, copper induced proteinase K resistance and increase of DNA binding affinity on native sperm H1 histones. These observations are consistent with a copper induced reorganization of the side-chains of arginine residues. Copper, instead, did not affect DNA binding affinity of somatic and deguanidinated H1 histones, which show similar K/R ratio and DNA binding mode. These results indicate that arginine residues could affect these H1 histones properties and provide new insights into copper toxicity mechanisms.
format	article
author	Marina Piscopo Marco Trifuoggi Carmela Scarano Carla Gori Antonella Giarra Ferdinando Febbraio
author_facet	Marina Piscopo Marco Trifuoggi Carmela Scarano Carla Gori Antonella Giarra Ferdinando Febbraio
author_sort	Marina Piscopo
title	Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
title_short	Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
title_full	Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
title_fullStr	Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
title_full_unstemmed	Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones
title_sort	relevance of arginine residues in cu(ii)-induced dna breakage and proteinase k resistance of h1 histones
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/fc102ad6da5641df870dfccbaeeaf859
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Relevance of arginine residues in Cu(II)-induced DNA breakage and Proteinase K resistance of H1 histones

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