Unknown

Dataset Information

0

Charting the native architecture of Chlamydomonas thylakoid membranes with single-molecule precision.


ABSTRACT: Thylakoid membranes scaffold an assortment of large protein complexes that work together to harness the energy of light. It has been a longstanding challenge to visualize how the intricate thylakoid network organizes these protein complexes to finely tune the photosynthetic reactions. Previously, we used in situ cryo-electron tomography to reveal the native architecture of thylakoid membranes (Engel et al., 2015). Here, we leverage technical advances to resolve the individual protein complexes within these membranes. Combined with a new method to visualize membrane surface topology, we map the molecular landscapes of thylakoid membranes inside green algae cells. Our tomograms provide insights into the molecular forces that drive thylakoid stacking and reveal that photosystems I and II are strictly segregated at the borders between appressed and non-appressed membrane domains. This new approach to charting thylakoid topology lays the foundation for dissecting photosynthetic regulation at the level of single protein complexes within the cell.

SUBMITTER: Wietrzynski W 

PROVIDER: S-EPMC7164959 | BioStudies | 2020-01-01

REPOSITORIES: biostudies

Similar Datasets

2012-01-01 | S-EPMC3499227 | BioStudies
2020-01-01 | S-EPMC7175462 | BioStudies
2011-01-01 | S-EPMC3355511 | BioStudies
2017-01-01 | S-EPMC5683893 | BioStudies
2020-01-01 | S-EPMC7444523 | BioStudies
1998-01-01 | S-EPMC1170505 | BioStudies
2018-01-01 | S-EPMC6150804 | BioStudies
2017-01-01 | S-EPMC5577252 | BioStudies
1000-01-01 | S-EPMC1464369 | BioStudies
2020-01-01 | S-EPMC7291772 | BioStudies