Sychronized cells as a model for the diel regulation of Rubisco-EPYC1 interactions in the Chlamydomonas CCM

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• Indu Santhanagopalan, Griffiths lab
• Thursday 31 January 2019, 13:00-13:30
• Department of Plant Sciences, Large Lecture Theatre.

If you have a question about this talk, please contact Ronelle Roth.

Pyrenoids present in chloroplast stroma of most eukaryotic algae have been identified as the center for biophysical carbon concentration mechanism. The pyrenoids are delineated by a starch sheath, with the majority of Rubisco aggregated around a knot of thylakoid tubules, which also allow the exchange of photosynthetic substrates and metabolites. Mass spectrometric and co-localization studies with the model alga Chlamydomonas reinhardtii have helped identify EPYC1 as a linker molecule for Rubisco with in the pyrenoid (Mackinder et al., 2016). EPYC1 is a serine-rich, highly basic 35 kDa protein of low complexity containing four repeats, that gets extensively phosphorylated. Most studies focus on the induction of the CCM under low CO2 , but the pyrenoid and CCM components are regulated dynamically during the day-night cycle (Mitchell et al., 2014). In this study, we have explored the diurnal variation in post-translational phosphorylation modifications of EPYC1 in synchronized cultures of C. reinhardtii, and have determined how EPYC1 is differentially phosphorylated across the diurnal cycle by using gel-based assays. The availability of diurnal transcriptomic data for C. reinhardtii (Zones et al., 2015) has made it possible for us to align the expression profiles of potential kinases and phosphatases that might be involved in phosphorylation and dephosphorylation of EPYC1 . We identified a number of potential candidates and have undertaken additional work to characterize their expression and interaction with EPYC1 phosphorylation. The study provides additional insights for the mechanisms underlying the regulation of pyrenoid formation and EPYC1 -Rubisco interactions.

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