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They are relatively small proteins that contain up to three transmembrane domains (TM) and show high copper specificity for reduced copper (Cu +) ( Puig et al., 2002 Petris, 2004). High Cu concentrations, in turn, result in ScMac1 inactivation ( Zhu et al., 1998).Ĭopper is transported inside the cell by two high affinity copper transporter proteins (Ctr) localized at the plasma membrane, ScCtr1 and ScCtr3 ( Pena et al., 2000). In the absence of copper, ScMac1 is able to bind DNA, thereby activating the expression of the high affinity Cu uptake system. The expression of the high affinity Cu uptake system is transcriptionally regulated by a copper metalloregulatory transcription factor (CuMRTF) named ScMac1 ( Labbe et al., 1997 Keller et al., 2005). An efficient copper uptake system has been proved to be critical to cover basic cellular needs of the cation. Homeostasis studies in Saccharomyces cerevisiae, first lead to the identification of genes responsible for Cu uptake, distribution to cellular compartments and detoxification ( Culotta et al., 1994 Lin et al., 1997 Pena et al., 1998). They include copper uptake, intracellular traffic, storage, and detoxification processes ( Balamurugan and Schaffner, 2006 Nevitt et al., 2012).
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Hence, all organisms have elaborate mechanisms that secure copper bioavailability, yet maintain free copper levels below the toxicity threshold. However, free intracellular copper can interfere with red-ox processes generating reactive oxygen species (ROS) or cause metalloprotein dysfunction by displacement of other bound metal ions ( Fridovich, 1983 Macomber and Imlay, 2009 Besold et al., 2016). Its capacity to adopt an oxidized (Cu 2+) and a reduced (Cu +) state is exploited by many enzymes to act as redox cofactor in enzyme catalyzed processes ( Nevitt et al., 2012) cytochrome c, a key component of mitochondrial cellular respiration process superoxide dismutase, for ROS neutralization laccases, a protein family with great biotechnology implications which are involved in fungal pigment synthesis and lysil oxidase for collagen maturation, for example ( Scherer and Fischer, 2001 Lutsenko, 2010 Ding et al., 2011 Smith et al., 2017). Altogether, our results support the view that AnCtrC plays a major role in covering the nutritional copper requirements and AnCtrA acts as a specific transporter for extreme copper deficiency scenarios.Ĭopper (Cu) is an indispensable trace element for most living organisms. Although both proteins partially localized at the plasma membrane, AnCtrC was visible at membranes that resembled the ER, whilst a substantial pool of AnCtrA accumulated in vesicular structures resembling endosomes. Each transporter followed a characteristic expression and cellular localization pattern. In mild copper deficiency conditions, the null mutant of AnctrC resulted in secondary level copper limitation effects, while deletion of AnctrA resulted in primary level copper limitation effects under extreme copper scarcity conditions. The same study allowed for the deeper characterization of the two high-affinity copper transporters: AnCtrA and AnCtrC.
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An RNA-seq screen in standard growth and copper toxicity conditions revealed expression changes in key copper response elements, providing an insight into their coordinated functions.
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This study expands on various aspects of the system in the model filamentous fungus Aspergillus nidulans. Microbial Biochemistry Laboratory, Department of Applied Chemistry, Faculty of Chemistry, University of the Basque Country, San Sebastian, SpainĬopper ion homeostasis involves a finely tuned and complex multi-level response system.Martzel Antsotegi-Uskola *, Ane Markina-Iñarrairaegui and Unai Ugalde