Project description:In the model green alga Chlamydomonas (Chlamydomonas reinhardtii), the synthesis of several chloroplast-encoded photosynthetic subunits is feedback-regulated by the assembly state of the respective protein complex. This regulation is known as control by epistasy of synthesis (CES) and matches protein synthesis with the requirements of protein complex assembly in photosystem II (PSII), the cytochrome b6f complex (Cyt b6f), photosystem I (PSI), ATP synthase and Rubisco . In embryophytes, however, CES was only described to coordinate synthesis of the large and small subunits of Rubisco, raising the question if additional CES mechanisms exist in land plants or if stoichiometric photosynthetic protein accumulation is only achieved by the wasteful degradation of excess subunits. We systematically examined suitable tobacco and Arabidopsis mutants with assembly defects in PSII, PSI, Cyt b6f complex, ATP synthase, NDH (NAD(P)H dehydrogenase-like) complex and Rubisco for feedback regulation. Thereby, we validated the CES in Rubisco and uncovered translational feedback regulation in PSII, involving psbA, psbB, psbD and psbH and in Cyt b6f, connecting PetA and PetB protein synthesis. Remarkably, some of these feedback regulation mechanisms are not conserved between the green alga and embryophytes. Our data do not provide any evidence for CES in PSI, ATP synthase or NDH complex assembly in embryophytes. In addition, our data disclose translational feedback regulation adjusting PSI levels with PSII accumulation. Overall, we discovered commonalities and differences in assembly-dependent feedback regulation of photosynthetic complexes between embryophytes and green algae.
Project description:Photosystem I (PSI) enables photo-electron transfer and regulates photosynthesis in the bioenergetic membranes of cyanobacteria and chloroplasts. Being a multi-subunit complex, its macromolecular organization affects the dynamics of photosynthetic membranes. Here we reveal a chloroplast PSI from the green alga Chlamydomonas reinhardtii that is organized as a homodimer.
Project description:Photosystem I (PSI) enables photo-electron transfer and regulates photosynthesis in the bioenergetic membranes of cyanobacteria and chloroplasts. Being a multi-subunit complex, its macromolecular organization affects the dynamics of photosynthetic membranes. Here we reveal a chloroplast PSI from the green alga Chlamydomonas reinhardtii that is organized as a homodimer.
Project description:Different high temperatures adversely affect crop and algal yields with various responses in photosynthetic cells. The list of genes required for thermotolerance remains elusive. Additionally, it is unclear how carbon source availability affects heat responses in plants and algae. We utilized the insertional, indexed, genome-saturating mutant library of the unicellular, eukaryotic green alga Chlamydomonas reinhardtii to perform genome-wide, quantitative, pooled screens under moderate (35oC) or acute (40oC) high temperatures with or without organic carbon sources. We identified heat-sensitive mutants based on quantitative growth rates and identified putative heat tolerance genes (HTGs). By triangulating HTGs with heat-induced transcripts or proteins in wildtype cultures and MapMan functional annotations, we present a high/medium-confidence list of 933 Chlamydomonas genes with putative roles in heat tolerance. Triangulated HTGs include those with known thermotolerance roles and novel genes with little or no functional annotation. About 50% of these high-confidence HTGs in Chlamydomonas have orthologs in green lineage organisms, including crop species. Arabidopsis thaliana mutants deficient in the ortholog of a high-confidence Chlamydomonas HTG were also heat sensitive. This work expands our knowledge of heat responses in photosynthetic cells and provides engineering targets to improve thermotolerance in algae and crops.
Project description:a chromosome-level nuclear genome and organelle genomes of the alpine snow alga Chloromonas typhlos were sequenced and assembled by integrating short- and long-read sequencing and proteogenomic strategy