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Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Ecoli]

ABSTRACT: We found that cyanobacterial RNA polymerase possesses very efficient intrinsic proofreading ability. This ability allows model species of cyanobacteria, Synechocystis sp PCC 6803 to keep in vivo level of transcriptional mistakes close to that of E.coli.

ORGANISM(S): Escherichia coli K-12

PROVIDER: GSE115132 | GEO | 2018/08/15

REPOSITORIES: GEO

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Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Synechoscystis sp]

Project description:We found that cyanobacterial RNA polymerase possesses very efficient intrinsic proofreading ability. This ability allows model species of cyanobacteria, Synechocystis sp PCC 6803 to keep in vivo level of transcriptional mistakes close to that of E.coli.

2018-08-15 | GSE115134 | GEO

Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Ecoli]

Project description:Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Ecoli]

| PRJNA473847 | ENA

Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors

Project description:Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors

| PRJNA473848 | ENA

Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Synechoscystis sp]

Project description:Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors [Synechoscystis sp]

| PRJNA473849 | ENA

The cyanobacterial phytochrome 2 regulates the expression of motility-related genes through the second messenger cyclic di-GMP

Project description:The cyanobacterial phytochrome Cph2 is a light-dependent diguanylate cyclase producing the second messenger c-di-GMP. Under blue light, the Cph2-dependent increase in the cellular c-di-GMP concentration leads to inhibition of motility in the cyanobacterium Synechocystis 6803. However, the targets of c-di-GMP in this cyanobacterium and its mechanism of action remained unclear. Here, we determined the cellular concentrations of three cyclic nucleotides in wild-type and Δcph2 cells after blue- and green light illumination. Inactivation of the photoreceptor gene completely abolished the blue-light dependent increase in the c-di-GMP content. Microarray analysis revealed that in the wild type in comparison to the Δcph2 mutant, blue light mainly led to a change in accumulation of mRNAs encoding minor pilins, putative chaperone usher pili as well as several chemotaxis regulators. The mRNA encoding the minor pilins pilA5-pilA6 is negatively affected by high c-di GMP content under blue light, whereas the minor pilin encoding operon pilA9-slr2018 accumulates under the same conditions, suggesting opposing functions of the respective gene sets. Based on mutational and gene expression analysis, we further suggest that the second Synechocystis 6803 homolog of a CRP-like transcription factor, SyCRP2, is the regulator of minor pilin gene expression and of putative chaperone usher pili genes slr1667/slr1668. Thus, our work indicates that the Cph2-mediated increase in cellular c-di-GMP concentration upon blue-light illumination specifically changes the transcriptome of Synechocystis 6803.

2020-03-23 | GSE116409 | GEO

Evidence for a major role of antisense RNAs in cyanobacterial gene regulation

Project description:The model cyanobacterium Synechocystis sp. PCC 6803 was used for a systematic survey on the number and types of antisense (as)RNAs. A tiled microarray was constructed with probes for both strands of the genes or intergenic spacers with candidate transcripts predicted by an algorithm and an equally sized and distributed control set. The resulting 102,739 individual probes cover an accumulated length of 1,441,146 nt or about 40% of the total chromosome sequence of Synechocystis 6803. Hybridization of this array with total RNA isolated from cultures raised under different growth conditions identified a high number of transcripts from intergenic spacers and in antisense orientation to known genes (natural cis-asRNAs). Extrapolated to the whole genome, around 10% of all open reading frames in Synechocystis 6803 may have a corresponding asRNA, suggesting a much more important role of chromosomally encoded asRNAs in bacteria then anticipated so far. Keywords: stress response 4 RNA hybridizations, 2 DNA controls. The raw data from the DNA hybridizations are in the GSE14410_DNA_1.txt and GSE14410_DNA_2.txt files.

2010-05-14 | E-GEOD-14410 | biostudies-arrayexpress

Evidence for a major role of antisense RNAs in cyanobacterial gene regulation

2009-01-14 | GSE14410 | GEO

The gene sml0013 of Synechocystis sp. strain PCC 6803 encodes for a novel subunit of the NDH1 complex that is ubiquitous distributed among cyanobacteria.

Project description:The NDH1 complex fulfils numerous tasks in the cyanobacterial cell such as respiration, cyclic electron flow, and inorganic carbon concentration. Despite the immense progress in our understanding of structure/function relation of the cyanobacterial NDH1 complex, the subunits catalysing the NAD(P)H docking and oxidation are still missing. The gene sml0013 of Synechocystis 6803 encodes for a small protein of unknown function for that homologs exist in all completely known cyanobacterial genomes. The protein exhibits weak similarities to the NDF6 protein, which was reported from Arabidopsis chloroplasts as a NDH subunit (Ishikawa et al. 2008). A sml0013 inactivation mutant of Synechocystis 6803 was generated and characterized. It showed only weak differences regarding growth and pigmentation at various culture conditions; most remarkably it exhibited a glucose-sensitive phenotype in the light. The genome-wide expression pattern of the M-NM-^Tsml0013::Km mutant was almost identical to wild type when grown under high CO2 conditions as well as after shifts to low CO2 conditions. However, measurements of the photosystem I redox kinetic in cells of the M-NM-^Tsml0013::Km mutant revealed differences to wild type such as a decreased capability of cyclic electron flow as well as of utilization of electrons from catabolic processes. These results suggest that the Sml0013 protein (named NdhP) represent a novel subunit of the cyanobacterial NDH1 complex mediating its coupling to the respiratory or photosynthetic electron flow. Gene expression of Synechocystis sp. PCC 6803 WT and a M-NM-^Tsml0013::Km mutant was monitored at HC conditions (5% CO2) and at 24h after a shift to LC conditions (ambient air containing 0.035% CO2). Each condition was sampled in biological duplicates.

2013-06-29 | E-GEOD-48415 | biostudies-arrayexpress

The gene sml0013 of Synechocystis sp. strain PCC 6803 encodes for a novel subunit of the NDH1 complex that is ubiquitous distributed among cyanobacteria.

Project description:The NDH1 complex fulfils numerous tasks in the cyanobacterial cell such as respiration, cyclic electron flow, and inorganic carbon concentration. Despite the immense progress in our understanding of structure/function relation of the cyanobacterial NDH1 complex, the subunits catalysing the NAD(P)H docking and oxidation are still missing. The gene sml0013 of Synechocystis 6803 encodes for a small protein of unknown function for that homologs exist in all completely known cyanobacterial genomes. The protein exhibits weak similarities to the NDF6 protein, which was reported from Arabidopsis chloroplasts as a NDH subunit (Ishikawa et al. 2008). A sml0013 inactivation mutant of Synechocystis 6803 was generated and characterized. It showed only weak differences regarding growth and pigmentation at various culture conditions; most remarkably it exhibited a glucose-sensitive phenotype in the light. The genome-wide expression pattern of the Δsml0013::Km mutant was almost identical to wild type when grown under high CO2 conditions as well as after shifts to low CO2 conditions. However, measurements of the photosystem I redox kinetic in cells of the Δsml0013::Km mutant revealed differences to wild type such as a decreased capability of cyclic electron flow as well as of utilization of electrons from catabolic processes. These results suggest that the Sml0013 protein (named NdhP) represent a novel subunit of the cyanobacterial NDH1 complex mediating its coupling to the respiratory or photosynthetic electron flow.

2013-06-29 | GSE48415 | GEO

Active site of cyanobacterial RNA polymerase compensates for the absence of proofreading factors

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

2018-08-15 | GSE115135 | GEO