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Biology subjects

Heidig, S.-L.

Publications and source records attributed to Heidig, S.-L..

3 recordsLinked to original sources

Polyploid Achromatium sp. expresses protein variants based on environmental cues

Achromatium spp. are giant bacteria harboring hundreds of non-clonal chromosomes per cell. The allelic divergence they exhibit could be a mechanism to enable fine-tuned responses to environmental changes, enabling this organism to broaden its ecological range. However, while ubiquitous in freshwater and marine environments, Achromatium has not been obtained in culture, leaving the role and functioning of its genomic and proteomic diversity poorly understood. Here, we incubated freshly collected freshwater Achromatium under three temperature conditions to conduct comparative mass spectrometry-based proteomics experiments. These were interpreted against an Achromatium-specific protein atlas developed from curated published and new assemblies from marine and freshwater environments. This de novo assembled atlas allowed a twenty-fold increase in the number of identified proteins compared to mass spectrometry data searches against the UniProt database. Predicted proteins from the Achromatium atlas were grouped into orthologs, 5% of which showed temperature-associated detection of distinct protein variants within the group. This provides the first indication that Achromatium uses distinct protein variants under different environmental conditions, enabling it to swiftly respond to environmental changes through differential expression from its cache of chromosomes.

microbiology↗

Proteomic insights into the photobiology of the Hawaiian rice coral Montipora capitata in response to decreased light intensity

Reef-building corals are sessile marine organisms that inhabit a wide range of light habitats along depth gradients. As coral biology is often studied in the context of global change and changing temperatures, knowledge gaps persist in our understanding of the molecular and cellular pathways involved in the responses to other factors than temperature, such as light intensity, which decreases exponentially in the water column and gradually changes the environment. To fill this gap, we tested the response of the Hawaiian rice coral Montipora capitata to decreased light intensity in a field experiment in K[a]neohe Bay, Oahu, Hawaii, using Data-Independent Acquisition (DIA) proteomics. There was a significant effect of light intensity on both the coral and zooxanthellae proteomes. In the M. capitata host, 69 proteins differed significantly in abundance between light levels after two years. The 50 proteins identified as significantly more abundant in the control condition were mostly involved in mRNA and RNA processing, pointing toward a positive correlation between metabolic activity, growth rates and increased light levels. The 19 proteins identified as significantly more abundant in the shade treatment were associated with calcium transport and with the structure of key cellular components, such as cell membrane and cytoskeleton. By contrast, zooxanthellae showed only minor changes in protein abundances, with photosynthesis proteins more abundant in the shade treatment and enzymes involved in fatty acid metabolism more abundant in the control treatment. Overall, these findings establish a baseline for our understanding of the cellular and metabolic processes driving Montipora capitatas acclimatization potential to different light intensities.

ecology↗

New Swiss-knife activities of GroEL/Hsp60 proteins

GroEL/Hsp60 chaperonins are key proteins that control cell metabolism, stress adaptation and survival. They usually form a tetradecameric structure that assists, coupled to ATP hydrolysis, 10% of all cellular protein folding. Using recombinant E. coli, human mitochondrial and M. tuberculosis chaperonins, we found that these proteins have thioesterase, esterase and even, for some of them, auto-acyltransferase activities. The smaller oligomers of Hsp60 and M. tuberculosis GroEL1 were more prone to use the long acyl carbon chain substrate palmitoyl-CoA compared to tetradecameric E. coli GroEL and Hsp60. Enzymatic competition and replacement of M. tuberculosis GroEL1 residues allow identifying Asp86 and Thr89 in the ATP-binding pocket and an additional Ser393 influencing the thioesterase activity. Additionally, M. tuberculosis GroEL1 might enhance palmitoylation of the PpsE protein, which plays a role in the phthiocerol dimycocerosate (PDIM) biosynthesis. This could explain at least partly the involvement of GroEL1 in PDIM biosynthesis and antibiotic resistance.

biochemistry↗