scholarly journals Copper trafficking in the CsoR regulon of Streptomyces lividans

Metallomics ◽  
2015 ◽  
Vol 7 (1) ◽  
pp. 145-155 ◽  
Author(s):  
Amanda K. Chaplin ◽  
Benedict G. Tan ◽  
Erik Vijgenboom ◽  
Jonathan A. R. Worrall
Keyword(s):  
Streptomyces Lividans ◽  
Copper Chaperones ◽  
Copper Trafficking ◽  
Cu Stress

In Streptomyces lividans four copZ genes are present encoding CopZ copper chaperones. Under Cu stress CopZ can traffic Cu(i) to CsoR leading to the up-regulation of the CsoR regulon.

scholarly journals Copper in plants

2005 ◽  
Vol 17 (1) ◽  
pp. 145-156 ◽  
Author(s):  
Inmaculada Yruela
Keyword(s):  
Plant Growth ◽  
Copper Toxicity ◽  
Photosynthetic Electron Transport ◽  
Copper Level ◽  
Copper Chaperones ◽  
Copper Trafficking ◽  
Cellular Processes ◽  
Copper Transporters ◽  
Physiological Processes ◽  
Excess Copper

Copper is an essential metal for normal plant growth and development, although it is also potentially toxic. Copper participates in numerous physiological processes and is an essential cofactor for many metalloproteins, however, problems arise when excess copper is present in cells. Excess copper inhibits plant growth and impairs important cellular processes (i.e., photosynthetic electron transport). Since copper is both an essential cofactor and a toxic element, involving a complex network of metal trafficking pathways, different strategies have evolved in plants to appropriately regulate its homeostasis as a function of the environmental copper level. Such strategies must prevent accumulation of the metal in the freely reactive form (metal detoxification pathways) and ensure proper delivery of this element to target metalloproteins. The mechanisms involved in the acquisition of this essential micronutrient have not been clearly defined although a number of genes have recently been identified which encode potential copper transporters. This review gives a briefly overview of the current understanding of the more important features concerning copper toxicity and tolerance in plants, and brings information of recent findings on copper trafficking including copper detoxification factors, copper transporters and copper chaperones.

scholarly journals Cmc1p Is a Conserved Mitochondrial Twin CX9C Protein Involved in Cytochrome c Oxidase Biogenesis

2008 ◽  
Vol 28 (13) ◽  
pp. 4354-4364 ◽  
Author(s):  
Darryl Horn ◽  
Hassan Al-Ali ◽  
Antoni Barrientos
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Superoxide Dismutase ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Enzymes ◽  
Intermembrane Space ◽  
Mitochondrial Matrix ◽  
Copper Chaperones ◽  
Copper Trafficking ◽  
Mitochondrial Inner Membrane ◽  
Copper Incorporation

ABSTRACT Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). Copper incorporation into these enzymes is facilitated by metallochaperone proteins which probably use copper from a mitochondrial matrix-localized pool. Here we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function affects both COX and Sod1p. In Saccharomyces cerevisiae, Cmc1p localizes to the mitochondrial inner membrane facing the intermembrane space. Cmc1p is essential for full expression of COX and respiration, contains a twin CX9C domain conserved in other COX assembly copper chaperones, and has the ability to bind copper(I). Additionally, mutant cmc1 cells display increased mitochondrial Sod1p activity, while CMC1 overexpression results in decreased Sod1p activity. Our results suggest that Cmc1p could play a direct or indirect role in copper trafficking and distribution to COX and Sod1p.

scholarly journals Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans

2014 ◽  
Vol 459 (3) ◽  
pp. 525-538 ◽  
Author(s):  
Katie L. I. M. Blundell ◽  
Michael A. Hough ◽  
Erik Vijgenboom ◽  
Jonathan A. R. Worrall
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Streptomyces Lividans ◽  
Morphological Development ◽  
Copper Trafficking ◽  
Trafficking Pathway

A branched copper-trafficking pathway exists in Streptomyces livdians. One branch requires the metallochaperones Sco and ECuC to metallate the CuA domain of cytochrome c oxidase, with the second branch requiring only Sco to initiate a morphological development switch.

Identification and functional expression of ctaA, a P-type ATPase gene involved in copper trafficking in Trametes versicolor

Microbiology ◽  
2003 ◽  
Vol 149 (8) ◽  
pp. 2039-2048 ◽  
Author(s):  
Andreas Uldschmid ◽  
Renate Dombi ◽  
Karin Marbach
Keyword(s):  
Trametes Versicolor ◽  
Fold Increase ◽  
Functional Expression ◽  
Laccase Production ◽  
Copper Chaperones ◽  
Copper Trafficking ◽  
Atpase Gene ◽  
In The Wild ◽  
Copper Distribution ◽  
P Type

Here the identification and characterization of a gene encoding a copper-trafficking enzyme, ctaA (copper-transporting ATPase), from the basidiomycete Trametes versicolor are described. This P-type copper ATPase gene has two alleles, differing primarily in the length of the second, unusually long intron, and encodes a 983 aa protein with 40 % sequence identity to yeast Ccc2p. Overexpression of ctaA in yeast grown in the presence of copper led to a 15-fold increase in laccase yields, while overexpression of ctaA and tahA, a previously identified copper homeostasis gene of T. versicolor, was additive, leading to a 20-fold increase in laccase production. In T. versicolor, overexpression of ctaA and tahA led to an eightfold increase in laccase expression, and a cotransformant still expressed laccase at 3000 μM copper when hardly any laccase activity is detected in the wild-type strain. Apparently, at low to moderate levels of copper tahA and ctaA overexpression disturbs the normal hierarchy of copper distribution, resulting in more being directed to the Golgi, while with high copper amounts that normally switch on the copper detoxification processes, tahA and ctaA gene products seem to out-compete the metallothionein copper chaperones, meaning laccase is still supplied with copper. These results may lead to a better understanding of copper trafficking and the hierarchy of copper distribution in the cell, and possibly be useful for constructing laccase-overproducing strains for biotechnological purposes.

Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24

Extremophiles ◽  
2021 ◽  
Author(s):  
Xin Chang ◽  
Shuang Wu ◽  
Jie Chen ◽  
Shengqi Xiong ◽  
Peng Wang ◽  
...  
Keyword(s):  
Streptomyces Lividans ◽  
Alkali Stability

scholarly journals Environmental Conditions Modulate the Transcriptomic Response of Both Caulobacter crescentus Morphotypes to Cu Stress

2021 ◽  
Vol 9 (6) ◽  
pp. 1116
Author(s):  
Laurens Maertens ◽  
Pauline Cherry ◽  
Françoise Tilquin ◽  
Rob Van Houdt ◽  
Jean-Yves Matroule
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Stress Responses ◽  
Caulobacter Crescentus ◽  
Oxidative Stress Response ◽  
Transport Systems ◽  
Transcriptomic Response ◽  
Swarmer Cell ◽  
Cu Stress ◽  
Cellular Environment

Bacteria encounter elevated copper (Cu) concentrations in multiple environments, varying from mining wastes to antimicrobial applications of copper. As the role of the environment in the bacterial response to Cu ion exposure remains elusive, we used a tagRNA-seq approach to elucidate the disparate responses of two morphotypes of Caulobacter crescentus NA1000 to moderate Cu stress in a complex rich (PYE) medium and a defined poor (M2G) medium. The transcriptome was more responsive in M2G, where we observed an extensive oxidative stress response and reconfiguration of the proteome, as well as the induction of metal resistance clusters. In PYE, little evidence was found for an oxidative stress response, but several transport systems were differentially expressed, and an increased need for histidine was apparent. These results show that the Cu stress response is strongly dependent on the cellular environment. In addition, induction of the extracytoplasmic function sigma factor SigF and its regulon was shared by the Cu stress responses in both media, and its central role was confirmed by the phenotypic screening of a sigF::Tn5 mutant. In both media, stalked cells were more responsive to Cu stress than swarmer cells, and a stronger basal expression of several cell protection systems was noted, indicating that the swarmer cell is inherently more Cu resistant. Our approach also allowed for detecting several new transcription start sites, putatively indicating small regulatory RNAs, and additional levels of Cu-responsive regulation.

scholarly journals The Phosin PptA Plays a Negative Role in the Regulation of Antibiotic Production in Streptomyces lividans

Antibiotics ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 325
Author(s):  
Noriyasu Shikura ◽  
Emmanuelle Darbon ◽  
Catherine Esnault ◽  
Ariane Deniset-Besseau ◽  
Delin Xu ◽  
...  
Keyword(s):  
Antibiotic Production ◽  
Streptomyces Lividans ◽  
Positive Control ◽  
Phosphate Limitation ◽  
Antibiotic Biosynthesis ◽  
Nudix Hydrolase ◽  
Energetic Stress ◽  
Accessory Factor ◽  
Negative Role ◽  
Weak Expression

In Streptomyces, antibiotic biosynthesis is triggered in phosphate limitation that is usually correlated with energetic stress. Polyphosphates constitute an important reservoir of phosphate and energy and a better understanding of their role in the regulation of antibiotic biosynthesis is of crucial importance. We previously characterized a gene, SLI_4384/ppk, encoding a polyphosphate kinase, whose disruption greatly enhanced the weak antibiotic production of Streptomyces lividans. In the condition of energetic stress, Ppk utilizes polyP as phosphate and energy donor, to generate ATP from ADP. In this paper, we established that ppk is co-transcribed with its two downstream genes, SLI_4383, encoding a phosin called PptA possessing a CHAD domain constituting a polyphosphate binding module and SLI_4382 encoding a nudix hydrolase. The expression of the ppk/pptA/SLI_4382 operon was shown to be under the positive control of the two-component system PhoR/PhoP and thus mainly expressed in condition of phosphate limitation. However, pptA and SLI_4382 can also be transcribed alone from their own promoter. The deletion of pptA resulted into earlier and stronger actinorhodin production and lower lipid content than the disruption of ppk, whereas the deletion of SLI_4382 had no obvious phenotypical consequences. The disruption of ppk was shown to have a polar effect on the expression of pptA, suggesting that the phenotype of the ppk mutant might be linked, at least in part, to the weak expression of pptA in this strain. Interestingly, the expression of phoR/phoP and that of the genes of the pho regulon involved in phosphate supply or saving were strongly up-regulated in pptA and ppk mutants, revealing that both mutants suffer from phosphate stress. Considering the presence of a polyphosphate binding module in PptA, but absence of similarities between PptA and known exo-polyphosphatases, we proposed that PptA constitutes an accessory factor for exopolyphosphatases or general phosphatases involved in the degradation of polyphosphates into phosphate.

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