Proteomics

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High-purity isolation and chemical composition of stabilisomes from thermophilic cyanobacteria


ABSTRACT: Thermophilic cyanobacteria are not only fundamental models for investigating thermotolerance mechanisms but also a valuable reservoir for the development of novel thermophilic bioresources. Progress in both of these areas, however, is contingent upon the precise characterization of their key subcellular organelles, such as the intracellular polyphosphate-rich granules which we term stabilisomes. The lack of a high-purity, structure-preserving isolation method has been a major technical bottleneck hindering such research. This study describes a high-fidelity, structure-preserving purification strategy, boosting the granule-to-protein yield by over 10,000-fold compared with conventional methods. The high fidelity of this method is confirmed by the retention of complex proteomic (937 proteins) and metabolomic (1,076 metabolites) signatures. Building on this, subsequent quantitative analysis across cyanobacteria at 7 hot spring sampling sites revealed a conserved core chemical composition dominated by polyphosphate (21.1%-36.4%), proteins (9.9%-20.0%), amino acids (1.6%-7.4%), and lipids (12.0%-21.0%), which nevertheless showed significant variabilitiy in the abundance of these components across species. This work establishes a robust methodological framework for isolating prokaryotic stress-responsive organelles, lays the foundation for mechanistic investigations into microbial adaptation, and serves as a prerequisite for exploring the biomedical applications of these organelles.

INSTRUMENT(S):

ORGANISM(S): Synechococcus Sp. M1

SUBMITTER: Chenyu Wang  

LAB HEAD: Chenyu, Wang

PROVIDER: PXD068468 | Pride | 2025-09-18

REPOSITORIES: Pride

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