Copper induction of lactate oxidase of Lactococcus lactis: a novel metal stress response

Barré, Olivier; Mourlane, Frédéric; Solioz, Marc (2007). Copper induction of lactate oxidase of Lactococcus lactis: a novel metal stress response. Journal of bacteriology, 189(16), pp. 5947-54. Washington, D.C.: American Society for Microbiology 10.1128/JB.00576-07

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Lactococcus lactis IL1403, a lactic acid bacterium widely used for food fermentation, is often exposed to stress conditions. One such condition is exposure to copper, such as in cheese making in copper vats. Copper is an essential micronutrient in prokaryotes and eukaryotes but can be toxic if in excess. Thus, copper homeostatic mechanisms, consisting chiefly of copper transporters and their regulators, have evolved in all organisms to control cytoplasmic copper levels. Using proteomics to identify novel proteins involved in the response of L. lactis IL1403 to copper, cells were exposed to 200 muM copper sulfate for 45 min, followed by resolution of the cytoplasmic fraction by two-dimensional gel electrophoresis. One protein strongly induced by copper was LctO, which was shown to be a NAD-independent lactate oxidase. It catalyzed the conversion of lactate to pyruvate in vivo and in vitro. Copper, cadmium, and silver induced LctO, as shown by real-time quantitative PCR. A copper-regulatory element was identified in the 5' region of the lctO gene and shown to interact with the CopR regulator, encoded by the unlinked copRZA operon. Induction of LctO by copper represents a novel copper stress response, and we suggest that it serves in the scavenging of molecular oxygen.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Service Sector > Institute of Clinical Pharmacology and Visceral Research [discontinued]
UniBE Contributor:	Barré, Olivier, Solioz, Marc
ISSN:	0021-9193
ISBN:	17557814
Publisher:	American Society for Microbiology
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:54
Last Modified:	05 Dec 2022 14:16
Publisher DOI:	10.1128/JB.00576-07
PubMed ID:	17557814
Web of Science ID:	000248584800018
URI:	https://boris.unibe.ch/id/eprint/22928 (FactScience: 37755)