<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Atkinson N</submitter><funding>Leverhulme Trust</funding><funding>RCUK | Biotechnology and Biological Sciences Research Council</funding><funding>Wellcome Trust</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>6303</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7726157</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(1)</volume><pubmed_abstract>Photosynthetic CO&lt;sub>2&lt;/sub> fixation in plants is limited by the inefficiency of the CO&lt;sub>2&lt;/sub>-assimilating enzyme Rubisco. In most eukaryotic algae, Rubisco aggregates within a microcompartment known as the pyrenoid, in association with a CO&lt;sub>2&lt;/sub>-concentrating mechanism that improves photosynthetic operating efficiency under conditions of low inorganic carbon. Recent work has shown that the pyrenoid matrix is a phase-separated, liquid-like condensate. In the alga Chlamydomonas reinhardtii, condensation is mediated by two components: Rubisco and the linker protein EPYC1 (Essential Pyrenoid Component 1). Here, we show that expression of mature EPYC1 and a plant-algal hybrid Rubisco leads to spontaneous condensation of Rubisco into a single phase-separated compartment in Arabid</pubmed_abstract><journal>Nature communications</journal><pubmed_title>Condensation of Rubisco into a proto-pyrenoid in higher plant chloroplasts.</pubmed_title><pmcid>PMC7726157</pmcid><funding_grant_id>RPG-2017-402</funding_grant_id><funding_grant_id>BB/S015337/1</funding_grant_id><funding_grant_id>WT104915MA</funding_grant_id><funding_grant_id>BB/S015531/1</funding_grant_id><pubmed_authors>Atkinson N</pubmed_authors><pubmed_authors>McCormick AJ</pubmed_authors><pubmed_authors>Chan KX</pubmed_authors><pubmed_authors>Mao Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Condensation of Rubisco into a proto-pyrenoid in higher plant chloroplasts.</name><description>Photosynthetic CO&lt;sub>2&lt;/sub> fixation in plants is limited by the inefficiency of the CO&lt;sub>2&lt;/sub>-assimilating enzyme Rubisco. In most eukaryotic algae, Rubisco aggregates within a microcompartment known as the pyrenoid, in association with a CO&lt;sub>2&lt;/sub>-concentrating mechanism that improves photosynthetic operating efficiency under conditions of low inorganic carbon. Recent work has shown that the pyrenoid matrix is a phase-separated, liquid-like condensate. In the alga Chlamydomonas reinhardtii, condensation is mediated by two components: Rubisco and the linker protein EPYC1 (Essential Pyrenoid Component 1). Here, we show that expression of mature EPYC1 and a plant-algal hybrid Rubisco leads to spontaneous condensation of Rubisco into a single phase-separated compartment in Arabid</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Dec</publication><modification>2025-04-22T13:40:47.78Z</modification><creation>2025-04-06T00:42:05.882Z</creation></dates><accession>S-EPMC7726157</accession><cross_references><pubmed>33298923</pubmed><doi>10.1038/s41467-020-20132-0</doi></cross_references></HashMap>