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Tullberg, C.

Publications and source records attributed to Tullberg, C..

2 recordsLinked to original sources

Role of Chloroplast Lipid-Remodelling Protein 23 During Cold Acclimation in Arabidopsis thaliana

Cold acclimation is a crucial physiological process that enables plants to adapt to low temperatures. A key aspect of this adaptation is lipid remodeling, which preserves membrane fluidity and integrity under cold stress. Proteins of the chloroplast envelope membranes are increasingly recognized for their role in acclimation to changing environmental conditions. While lipid synthesis occurs at the inner envelope membrane, little is known about specific proteins involved in lipid remodeling during cold acclimation. In this study, we investigate the role of Chloroplast Lipid Remodeling Protein 23 (CLRP23) as a component of the inner chloroplast envelope membrane. Subcellular fractionation combined with protease protection assays provided evidence for its orientation toward the intermembrane space. To explore its function, we analyzed the physiological performance and lipid composition in CLRP23-deficient mutant plants. Under cold stress, we observed significant impairments in photosynthesis and exaggerations in galactolipid response, suggesting CLRP23 is involved in lipid remodeling. Lipid overlay assays, supported by in silico docking analyses, demonstrate that CLRP23 can directly interact with chloroplast lipids, including galactolipids. Complementary transcriptomic and proteomic analyses reveal broader effects on cold-responsive pathways, supporting the view that CLRP23 contributes to the integration of membrane and metabolic responses during acclimation. These findings expand our understanding of protein-mediated processes during cold acclimation.

plant biology↗

Acinetobacter guillouiae strain isolated from sludge capable of partially degrade polyethylene terephthalate: genomic and biochemical insights

The escalating accumulation of plastic waste in terrestrial and aquatic ecosystems profoundly threatens environmental health and biodiversity while impacting human well-being. Recently, many microorganisms capable of degrading polyethylene terephthalate (PET) have been reported, primarily sourced from terrestrial soils and marine environments. Notably, the challenge of PET pollution in aquatic environments has remained a persistent research concern. In this study, we present the isolation and characterization of Acinetobacter guillouiae strain I-MWF, obtained from a wastewater treatment plant in Makri, AJK, Pakistan, using molecular phylogenetic analysis based on genome sequencing. Results revealed that this strain exhibits the ability for PET powder degradation, as confirmed by HPLC/LCMS analysis. Furthermore, we conducted whole-genome sequencing using Illumina technology and bioinformatically explored this strains potential repertoire of lipase and esterase enzymes. Under optimized conditions of 23{degrees}C and pH 7 in mineral salt media with PET powder as the sole organic substrate, A. guillouiae I-MWF could degrade partially. Extracellular enzymes yielded PET depolymerization products identified as mono(2- hydroxyethyl) terephthalic acid and terephthalic acid. The sequenced genome of this strain spans 4.61 Mb with a mean G + C content of 38.2%, containing 4,178 coding genes, 71 tRNA, and six rRNA genes. Although no cutinase-like enzymes were identified, our analysis unveiled a diverse array of putative lipases and three esterases, all sharing the typical /{beta} hydrolase fold. Additionally, comprehensive molecular modelling analysis suggested that some of the 18 identified extracellular hydrolases may be involved in polyester enzymatic depolymerization processes.

microbiology↗