AI Article Synopsis
- Some cyanobacteria adapt to low-light environments by expressing a specialized protein called allophycocyanin (AP) that absorbs far-red light (FRL).
- Using advanced imaging techniques, researchers found that this FRL-absorbing complex (FRL-AP) forms unique helical nanotubes instead of the usual circular shapes, due to changes in its structure.
- Although these nanotubes are less efficient in capturing light, their ability to absorb FRL under low visibility represents a valuable compromise, highlighting the diversity and adaptability of light-harvesting proteins in nature.
Article Abstract
To compete in certain low-light environments, some cyanobacteria express a paralog of the light-harvesting phycobiliprotein, allophycocyanin (AP), that strongly absorbs far-red light (FRL). Using cryo-electron microscopy and time-resolved absorption spectroscopy, we reveal the structure-function relationship of this FRL-absorbing AP complex (FRL-AP) that is expressed during acclimation to low light and that likely associates with chlorophyll a-containing photosystem I. FRL-AP assembles as helical nanotubes rather than typical toroids due to alterations of the domain geometry within each subunit. Spectroscopic characterization suggests that FRL-AP nanotubes are somewhat inefficient antenna; however, the enhanced ability to harvest FRL when visible light is severely attenuated represents a beneficial trade-off. The results expand the known diversity of light-harvesting proteins in nature and exemplify how biological plasticity is achieved by balancing resource accessibility with efficiency.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10038336 | PMC |
| http://dx.doi.org/10.1126/sciadv.adg0251 | DOI Listing |
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