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The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe

ABSTRACT: The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe

PROVIDER: PRJNA541560 | ENA |

REPOSITORIES: ENA

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The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [RNA-seq]

Project description:The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [RNA-seq]

| PRJNA541559 | ENA

The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [ChIP-seq]

Project description:The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [ChIP-seq]

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The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [RNA-seq]

Project description:RNA-seq to identify Loz1-dependent change in transcriptome in response to zinc supplementation.

2019-09-20 | GSE130845 | GEO

The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe [ChIP-seq]

Project description:ChIP-seq to determine if the DNA binding activity of Loz1 is dependent upon zinc.

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The zinc-responsive repressor Loz1 is the master regulator of zinc homeostasis in Schizosaccharomyces pombe

Project description:This SuperSeries is composed of the SubSeries listed below.

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Zinc-dependent regulation of the adh1 antisense transcript in fission yeast

Project description:In yeast, alcohol dehydrogenase I (Adh1) is an abundant zinc binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that is induced in response to zinc-limitation. This antisense transcript (adh1AS) shows a reciprocal expression pattern to that the adh1 mRNA partner. In this study we show that increased expression of the adh1AS transcript in zinc-limited cells is necessary for the repression of adh1 gene expression and that the increased level of the adh1AS transcript in zinc-limited cells is a result of two mechanisms. At the transcriptional level, the adh1AS transcript is expressed at a high level in zinc-limited cells. In addition to this transcriptional control, adh1AS transcripts preferentially accumulate in zinc-limited cells when the adh1AS transcript is expressed from a constitutive promoter. This secondary mechanism requires the simultaneous expression of adh1. Our studies reveal how multiple mechanisms can synergistically control the ratio of sense to antisense transcripts, and highlight a novel mechanism by which adh1 gene expression can be controlled by cellular zinc availability Sense and antisense expression of the S. pombe transcriptome was measured under zinc-limiting and zinc-replete conditions, using 3 replicates of each condition and an anti-RNA/DNA antibody labeling technique.

2012-12-12 | E-GEOD-39701 | biostudies-arrayexpress

The metalloregulatory site in Streptococcus pneumoniae AdcR, a zinc-activated MarR-family repressor

2010-10-01 | GSE21506 | GEO

The metalloregulatory site in Streptococcus pneumoniae AdcR, a zinc-activated MarR-family repressor

Project description:Streptococcus pneumoniae D39 AdcR (adhesion competence repressor) is the first metal-sensing member of the MarR (multiple antibiotic resistance repressor) family to be characterized. Expression profiling of a âadcR strain grown in liquid culture under microaerobic conditions revealed that transcript amounts for 13 genes were up-regulated relative to the wild-type strain, among them adcR, adcCBA, encoding a high affinity ABC uptake system for zinc, and genes encoding cell-surface zinc-binding pneumococcal histidine triad (pht) and adcII (lmb, laminin binding) proteins. Down-regulated transcripts included those encoding two putative zinc-containing alcohol dehydrogenases. Bacterial strains were grown exponentially in rich (BHI) media at 37C and an atmosphere of 5% CO2 to OD620~0.2, and were processed as described in the related Sample records. Samples were collected from three independent biological replicates and included one dye swap. Data were normalized using the Lowess (block) method without background subtraction. Changes in relative transcript amounts of positive or negative 2-fold with Bayesian P value of <0.001 were considered significant, and were included as supplementary material for the accompanying manuscript (The metalloregulatory site in Streptococcus pneumoniae AdcR, a zinc-activated MarR-family repressor; Reyes-Caballero, H. et al, manuscript in preparation).

2010-10-01 | E-GEOD-21506 | biostudies-arrayexpress

Zinc-dependent regulation of the adh1 antisense transcript in fission yeast

2012-12-12 | GSE39701 | GEO

An Extended dsRBD with a Novel Zinc-Binding Motif Mediates Nuclear Retention of Fission Yeast Dicer

Project description:Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast, disruption of zinc coordination renders Dcr1 mainly cytoplasmic and leads to remarkable changes in gene expression and loss of heterochromatin assembly. In summary, our results reveal novel insights into the mechanism of nuclear retention of Dcr1 and raise the possibility that this new class of dsRBDs might generally function in nucleo-cytoplasmic trafficking and not substrate binding. The C-terminal domain of Dcr1 constitutes a novel regulatory module that might represent a potential target for therapeutic intervention with fungal diseases. 12 chips representing 4 different strains. Every condition is represented by three biological replicates

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