Klebsormidium flaccidum strain:UTEX 321
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ABSTRACT:
PROVIDER: PRJNA51159 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:RNA-seq of Klebsormidium nitens NIES-2285 in the presence of IAA (NIES-2285 strain was taxonomically reclassified from K. flaccidum)
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Project description:genome sequence project of a filamentous terrestrial alga Klebsormidium nitens NIES-2285 (NIES-2285 strain was taxonomically reclassified from K. flaccidum)
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Project description:Klebsormidium crenulatum strain:SAG 2415 Transcriptome or Gene expression
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Project description:During the evolution of life on Earth, the conquest of land by plants played a pivotal role producing a boost in land biomass, a substantial drop in atmospheric CO2, an increase in oxygen and the emergence of new terrestrial habitats facilitating land colonization by animals. Therefore, the characterization of the molecular mechanisms that allowed plant terrestralization is a cornerstone in evolutionary studies. Viridiplantae or the green lineage is divided into two clades Chlorophyta or green microalgae and Streptophyta that in turn splits into Embryophyta or land plants and Charophyta. The latest are mainly considered aquatic algae although some facultative terrestrial species has been identified. Charophyta are generally accepted as the extant algal species most closely related to current land plants and, therefore, they are used in evolutionary studies on plant terrestralization. High light irradiance was one of the major stressors that ancestral charophytic algae needed to overcome during the transition from aquatic to terrestrial environments. In this study, we have chosen the facultative terrestrial early charophytic alga Klebsormidium nitens to perform an integrative transcriptomic and metabolomic analysis under high light in order to unveil key mechanisms involved in the early steps of plants terrestralization. We found a fast chloroplast retrograde signaling possibly mediated by reactive oxygen species and the inositol polyphosphate 1-phosphatase (SAL1) and 3′-phosphoadenosine-5′-phosphate (PAP) pathways inducing gene expression and accumulation of specific metabolites. Systems used by both Chlorophyta and Embryophyta were activated such as the xanthophyll cycle with an accumulation of zeaxanthin and protein folding and repair mechanisms constituted by NADPH-dependent thioredoxin reductases, thioredoxin-disulfide reductases and peroxiredoxins. Similarly, cyclic electron flow, specifically the pathway dependent on Proton Gradient Regulation 5, was strongly activated under high light. We detected a simultaneous co-activation of the non-photochemical quenching mechanisms based on LHC-like Stress Related protein and the photosystem II subunit S that are specific to Chlorophyta and Embryophyta respectively. Exclusive Embryophyta systems for the synthesis, sensing and response to the phytohormone auxin were also activated under high light in Klebsormidium leading to an increase in auxin content with the concomitant accumulation of amino acids such as tryptophan, histidine and phenylalanine.
2022-04-29 | GSE198330 | GEO
Project description:Transcriptomic Response to High Light in the Charophyte Klebsormidium nitens
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Project description:Freeze tolerant green alga belonging to Charophyceae
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Project description:When grown in green light, Fremyella diplosiphon strain UTEX 481 produces the red-colored protein phycoerythrin (PE) to maximize photosynthetic light harvesting. PE is composed of two subunits, CpeA and CpeB, which carry two and three phycoerythrobilin (PEB) chromophores, respectively, that are attached to specific Cys residues via thioether linkages. Specific bilin lyases are hypothesized to catalyze each PEB ligation. Using a heterologous, coexpression system in Escherichia coli, the PEB ligation activities of putative lyase subunits CpeY, CpeZ, and CpeS were tested on the CpeA and CpeB subunits from F. diplosiphon. Purified His(6)-tagged CpeA, obtained by coexpressing cpeA, cpeYZ, and the genes for PEB synthesis, had absorbance and fluorescence emission maxima at 566 and 574 nm, respectively. CpeY alone, but not CpeZ, could ligate PEB to CpeA, but the yield of CpeA-PEB was lower than achieved with CpeY and CpeZ together. Studies with site-specific variants of CpeA(C82S and C139S), together with mass spectrometric analysis of trypsin-digested CpeA-PEB, revealed that CpeY/CpeZ attached PEB at Cys(82) of CpeA. The CpeS bilin lyase ligated PEB at both Cys(82) and Cys(139) of CpeA but very inefficiently; the yield of PEB ligated at Cys(82) was much lower than observed with CpeY or CpeY/CpeZ. However, CpeS efficiently attached PEB to Cys(80) of CpeB but neither CpeY, CpeZ, nor CpeY/CpeZ could ligate PEB to CpeB.
| S-EPMC3195565 | biostudies-literature
Project description:Spirogyra pratensis transcriptome sequencing
| PRJNA51147 | ENA