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SUMMARY:Sychronized cells as a model for the diel regulation of Rubisco-EP
 YC1 interactions in the Chlamydomonas CCM - Indu Santhanagopalan\, Griffit
 hs lab
DTSTART:20190131T130000Z
DTEND:20190131T133000Z
UID:TALK116002@talks.cam.ac.uk
CONTACT:Ronelle Roth
DESCRIPTION:Pyrenoids present in chloroplast stroma of most eukaryotic alg
 ae have been identified as the center for biophysical carbon concentration
  mechanism. The pyrenoids are delineated by a starch sheath\, with the maj
 ority of Rubisco aggregated around a knot of thylakoid tubules\, which als
 o allow the exchange of photosynthetic substrates and metabolites. Mass sp
 ectrometric and co-localization studies with the model alga Chlamydomonas 
 reinhardtii have helped identify EPYC1 as a linker molecule for Rubisco wi
 th in the pyrenoid (Mackinder et al.\, 2016).  EPYC1 is a serine-rich\, hi
 ghly basic 35 kDa protein of low complexity containing four repeats\, that
  gets extensively phosphorylated. Most studies focus on the induction of t
 he CCM under low CO2\, but the pyrenoid and CCM components are regulated d
 ynamically during the day-night cycle (Mitchell et al.\, 2014). In this st
 udy\, we have explored the diurnal variation in post-translational phospho
 rylation modifications of EPYC1 in synchronized cultures of C. reinhardtii
 \, and have determined how EPYC1 is differentially phosphorylated across t
 he diurnal cycle by using gel-based assays. The availability of diurnal tr
 anscriptomic data for C. reinhardtii (Zones et al.\, 2015) has made it pos
 sible for us to align the expression profiles of potential kinases and pho
 sphatases that might be involved in phosphorylation and dephosphorylation 
 of EPYC1. We identified a number of potential candidates and have undertak
 en additional work to characterize their expression and interaction with E
 PYC1 phosphorylation. The study provides additional insights for the mecha
 nisms underlying the regulation of pyrenoid formation and EPYC1-Rubisco in
 teractions.
LOCATION:Department of Plant Sciences\, Large Lecture Theatre
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