Cop-like operon: Structure and organization in species of the Lactobacillale order

Copper is an essential and toxic trace metal for bacteria and, therefore, must be tightly regulated in the cell. Enterococcus hirae is a broadly studied model for copper homeostasis. The intracellular copper levels in E. hirae are regulated by the cop operon, which is formed by four genes: copA and...

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Autores principales:	REYES,ANGÉLICA, LEIVA,ANDREA, CAMBIAZO,VERÓNICA, MÉNDEZ,MARCO A, GONZÁLEZ,MAURICIO
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2006
Materias:	cop operon CopY binding site copper homeostasis Enterococcus hirae Lactobacillale order
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100010
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spelling	oai:scielo:S0716-976020060001000102006-06-30Cop-like operon: Structure and organization in species of the Lactobacillale orderREYES,ANGÉLICALEIVA,ANDREACAMBIAZO,VERÓNICAMÉNDEZ,MARCO AGONZÁLEZ,MAURICIO cop operon CopY binding site copper homeostasis Enterococcus hirae Lactobacillale order Copper is an essential and toxic trace metal for bacteria and, therefore, must be tightly regulated in the cell. Enterococcus hirae is a broadly studied model for copper homeostasis. The intracellular copper levels in E. hirae are regulated by the cop operon, which is formed by four genes: copA and copB that encode ATPases for influx and efflux of copper, respectively; copZ that encodes a copper chaperone; and copY, a copper responsive repressor. Since the complete genome sequence for E. hirae is not available, it is possible that other genes may encode proteins involved in copper homeostasis. Here, we identified a cop-like operon in nine species of Lactobacillale order with a known genome sequence. All of them always encoded a CopY-like repressor and a copper ATPase. The alignment of the cop-like operon promoter region revealed two CopY binding sites, one of which was conserved in all strains, and the second was only present in species of Streptococcus genus and L. johnsonii. Additional proteins associated to copper metabolism, CutC and Cupredoxin, also were detected. This study allowed for the description of the structure and organization of the cop operon and discussion of a phylogenetic hypothesis based on the differences observed in this operon's organization and its regulation in Lactobacillale order.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.39 n.1 20062006-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100010en10.4067/S0716-97602006000100010
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	cop operon CopY binding site copper homeostasis Enterococcus hirae Lactobacillale order
spellingShingle	cop operon CopY binding site copper homeostasis Enterococcus hirae Lactobacillale order REYES,ANGÉLICA LEIVA,ANDREA CAMBIAZO,VERÓNICA MÉNDEZ,MARCO A GONZÁLEZ,MAURICIO Cop-like operon: Structure and organization in species of the Lactobacillale order
description	Copper is an essential and toxic trace metal for bacteria and, therefore, must be tightly regulated in the cell. Enterococcus hirae is a broadly studied model for copper homeostasis. The intracellular copper levels in E. hirae are regulated by the cop operon, which is formed by four genes: copA and copB that encode ATPases for influx and efflux of copper, respectively; copZ that encodes a copper chaperone; and copY, a copper responsive repressor. Since the complete genome sequence for E. hirae is not available, it is possible that other genes may encode proteins involved in copper homeostasis. Here, we identified a cop-like operon in nine species of Lactobacillale order with a known genome sequence. All of them always encoded a CopY-like repressor and a copper ATPase. The alignment of the cop-like operon promoter region revealed two CopY binding sites, one of which was conserved in all strains, and the second was only present in species of Streptococcus genus and L. johnsonii. Additional proteins associated to copper metabolism, CutC and Cupredoxin, also were detected. This study allowed for the description of the structure and organization of the cop operon and discussion of a phylogenetic hypothesis based on the differences observed in this operon's organization and its regulation in Lactobacillale order.
author	REYES,ANGÉLICA LEIVA,ANDREA CAMBIAZO,VERÓNICA MÉNDEZ,MARCO A GONZÁLEZ,MAURICIO
author_facet	REYES,ANGÉLICA LEIVA,ANDREA CAMBIAZO,VERÓNICA MÉNDEZ,MARCO A GONZÁLEZ,MAURICIO
author_sort	REYES,ANGÉLICA
title	Cop-like operon: Structure and organization in species of the Lactobacillale order
title_short	Cop-like operon: Structure and organization in species of the Lactobacillale order
title_full	Cop-like operon: Structure and organization in species of the Lactobacillale order
title_fullStr	Cop-like operon: Structure and organization in species of the Lactobacillale order
title_full_unstemmed	Cop-like operon: Structure and organization in species of the Lactobacillale order
title_sort	cop-like operon: structure and organization in species of the lactobacillale order
publisher	Sociedad de Biología de Chile
publishDate	2006
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602006000100010
work_keys_str_mv	AT reyesangelica coplikeoperonstructureandorganizationinspeciesofthelactobacillaleorder AT leivaandrea coplikeoperonstructureandorganizationinspeciesofthelactobacillaleorder AT cambiazoveronica coplikeoperonstructureandorganizationinspeciesofthelactobacillaleorder AT mendezmarcoa coplikeoperonstructureandorganizationinspeciesofthelactobacillaleorder AT gonzalezmauricio coplikeoperonstructureandorganizationinspeciesofthelactobacillaleorder
_version_	1718441395511885824

Cop-like operon: Structure and organization in species of the Lactobacillale order

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