This work was made possible by my incredible mentors and support in the @Merchant_lab, the Niyogi lab (Masa Iwai and @khera_radhika) and the @NogalesLab (@GrobPatricia). We would also like to thank our collaborators @PNNLab and the facilities at @UCBerkeley.

We used #cryo-EM to solve the -Fe Dunaliella PSI-LHCI supercomplexes and found an additional LHCI tetramer with TIDI1. This eukaryotic PSI addition is like the isiA antenna ring in cyanobacteria showcasing a convergent evolution strategy to -Fe.

TIDI1 was previously shown to co-migrate with PSI subunits. When examining PSI subunits in whole cell proteomics data of +Fe vs -Fe cells, we noticed 3 light harvesting chlorophyll proteins (LHCA1, LHCA8, and LHCA7) are retained while other PSI subunits are downregulated in -Fe.

TIDI1 is a chlorophyll-binding protein that is highly induced during Fe starvation in Dunaliella spp. It is found in at least 4 other green algae species around the world and co-occurs with flavodoxin, an Fe-independent replacement for the Fe-dependent ferredoxin.