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Molecular insights into phycobilisome assembly pathway reveal crystalline bodies in cyanobacteria

Dahlgren, K.; Avramov, A.; Koke, E.; Iragavarapu, A. G.; Hren, A.; Acosta-Reyes, F. J.; Carl, A.; Herrmann, J.; Goldstein, L.; Spear, J.; Cameron, J. C.; Aydin, H.

2025-11-13 microbiology
10.1101/2025.11.13.688327 bioRxiv
Show abstract

In oxygenic photosynthetic organisms, light energy is converted to chemical energy to drive CO2 fixation reactions and sustain life on Earth. Cyanobacteria contain phycobilisome (PBS) complexes that play critical roles in light harvesting and directing light energy to the photosystem I and II reaction centers. The proper assembly of PBS components is an intricate process that is required for their activity and association with photosystem I and II. To understand the complex mechanisms regulating the PBS assembly, we knocked out the terminal emitter apcE, which forms the structural scaffold for the PBS core. ApcE knockout led to growth and pigment defects, including elevated levels of photosystem II and abnormal emission spectra. Light microscopy experiments revealed the accumulation of highly fluorescent puncta localized to the pole of apcE knockout cells. Further investigation using electron cryo-tomography identified highly repetitive crystalline arrays of densely packed PBS cylinders. Together, these data indicate that cyanobacteria may accumulate PBS components in the form of highly organized crystalline bodies as intermediates during PBS assembly.

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