Redox control of copper homeostasis in cyanobacteria

López‐Maury, Luis; Giner‐Lamia, Joaquín; Florencio, Francisco J.

doi:10.4161/psb.22323

Cited by 15 publications

(13 citation statements)

References 13 publications

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“…2A ; Table S1 ); unfortunately we can not distinguish between the two copies of these genes because of their high level of identity (>93% at nucleotide level) and we will refer to them simply as copMRS when analyzing gene expression. This observation also agrees with the fact that CopRS responds to copper released from plastocyanin degradation, in conditions that alter the photosynthetic electron flow, when cells were growing at this copper concentrations [21] , [35] . Although this induction is transitory and decreases 4 h after copper addition [21] , copM is also expressed when cells are cultured in BG11C containing copper ( Fig.…”

Section: Resultssupporting

confidence: 87%

Global Transcriptional Profiles of the Copper Responses in the Cyanobacterium Synechocystis sp. PCC 6803

2014

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Copper is an essential element involved in fundamental processes like respiration and photosynthesis. However, it becomes toxic at high concentration, which has forced organisms to control its cellular concentration. We have recently described a copper resistance system in the cyanobacterium Synechocystis sp. PCC 6803, which is mediated by the two-component system, CopRS, a RND metal transport system, CopBAC and a protein of unknown function, CopM. Here, we report the transcriptional responses to copper additions at non-toxic (0.3 µM) and toxic concentrations (3 µM) in the wild type and in the copper sensitive copR mutant strain. While 0.3 µM copper slightly stimulated metabolism and promoted the exchange between cytochrome c6 and plastocyanin as soluble electron carriers, the addition of 3 µM copper catalyzed the formation of ROS, led to a general stress response and induced expression of Fe-S cluster biogenesis genes. According to this, a double mutant strain copRsufR, which expresses constitutively the sufBCDS operon, tolerated higher copper concentration than the copR mutant strain, suggesting that Fe-S clusters are direct targets of copper toxicity in Synechocystis. In addition we have also demonstrated that InrS, a nickel binding transcriptional repressor that belong to the CsoR family of transcriptional factor, was involved in heavy metal homeostasis, including copper, in Synechocystis. Finally, global gene expression analysis of the copR mutant strain suggested that CopRS only controls the expression of copMRS and copBAC operons in response to copper.

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Section: Resultssupporting

confidence: 87%

Global Transcriptional Profiles of the Copper Responses in the Cyanobacterium Synechocystis sp. PCC 6803

2014

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“…Therefore, in contrast with other bacteria in which most of Cu 2+ -containing proteins are located in the plasma membrane or the periplasm, in cyanobacteria this metal is required at the thylakoid level, which imposes further complexity to its homeostasis [33][34][35][36]. In cyanobacteria, Cu 2+ is imported into the cell by a P 1 -type ATPase (CtaA), then chaperoned by Atx1 until the thylakoids, and finally transported into the thylakoids lumen by a second P 1 -type ATPase (PacS) [33,[35][36][37]. However, it is well established that an excess of Cu 2+ can be toxic to the cells by promoting the generation of ROS and/or competing for the binding sites of metallothioneins harboring other metals, impairing cell function and eventually causing cell death [29,38].…”

Section: Accepted Manuscriptmentioning

confidence: 93%

“…Cu 2+ is an essential micronutrient that acts as a cofactor for several proteins/enzymes, such as plastocyanin and cytochrome c oxidase, involved in the oxygenic photosynthetic electron transfer chain [33,34]. Therefore, in contrast with other bacteria in which most of Cu 2+ -containing proteins are located in the plasma membrane or the periplasm, in cyanobacteria this metal is required at the thylakoid level, which imposes further complexity to its homeostasis [33][34][35][36]. In cyanobacteria, Cu 2+ is imported into the cell by a P 1 -type ATPase (CtaA), then chaperoned by Atx1 until the thylakoids, and finally transported into the thylakoids lumen by a second P 1 -type ATPase (PacS) [33,[35][36][37].…”

Section: Accepted Manuscriptmentioning

confidence: 98%

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Effects of heavy metals on Cyanothece sp. CCY 0110 growth, extracellular polymeric substances (EPS) production, ultrastructure and protein profiles

Mota

Pereira

Meazzini

et al. 2015

Journal of Proteomics

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This work shows the holistic effects of different heavy metals on the cells of the highly efficient EPS-producer the cyanobacterium Cyanothece sp. CCY 0110. The growth/survival, EPS production, ultrastructure, protein profiles and stress response were evaluated. The knowledge generated by this study will contribute to the implementation of heavy-metal removal systems based on cyanobacteria EPS or their isolated polymers.

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“…PCC 6803 (hereafter referred to as Synechocystis; Tottey et al, 2001Tottey et al, , 2002Tottey et al, , 2008Badarau & Dennison, 2011). Recently, the genes encoding the Synechocystis TCS pair CopR-CopS and the periplasmic copper-binding protein CopM, as well as the copper-efflux pump CopBAC, have been ISSN 2059-7983 # 2016 International Union of Crystallography reported to be part of the copper-resistance system (Giner-Lamia et al, 2012Ló pez-Maury et al, 2012;Gittins, 2015). These six genes are clustered in the plasmid pSYSX and are organized into two operons: pcopMRS and copBAC.…”

Section: Introductionmentioning

confidence: 99%

Structural basis for copper/silver binding by theSynechocystismetallochaperone CopM

Zhao

Wang

Niu

et al. 2016

Acta Cryst Sect D Struct Biol

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Copper homeostasis integrates multiple processes from sensing to storage and efflux out of the cell. CopM is a cyanobacterial metallochaperone, the gene for which is located upstream of a two-component system for copper resistance, but the molecular basis for copper recognition by this four-helical bundle protein is unknown. Here, crystal structures of CopM in apo, copper-bound and silver-bound forms are reported. Monovalent copper/silver ions are buried within the bundle core; divalent copper ions are found on the surface of the bundle. The monovalent copper/silver-binding site is constituted by two consecutive histidines and is conserved in a previously functionally unknown protein family. The structural analyses show two conformational states and suggest that flexibility in the first α-helix is related to the metallochaperone function. These results also reveal functional diversity from a protein family with a simple four-helical fold.

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Redox control of copper homeostasis in cyanobacteria

Cited by 15 publications

References 13 publications

Global Transcriptional Profiles of the Copper Responses in the Cyanobacterium Synechocystis sp. PCC 6803

Global Transcriptional Profiles of the Copper Responses in the Cyanobacterium Synechocystis sp. PCC 6803

Effects of heavy metals on Cyanothece sp. CCY 0110 growth, extracellular polymeric substances (EPS) production, ultrastructure and protein profiles

Structural basis for copper/silver binding by theSynechocystismetallochaperone CopM

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