Presenting on “Revealing the Principles Behind Biomolecular Condensate Formation in Algal Pyrenoids”.

Trevor GrandPre, PhD, Schmidt Science Fellow, Princeton Center for Theoretical Science Fellow, Center for the Physics of Biological Function Fellow, Future Faculty in the Physical Sciences Fellow at Princeton University will speak on Thursday, September 12, 2024 at 10:00 am in Whitaker 218.

Abstract: Biomolecular condensates are membraneless organelles formed through the phase separation of macromolecules, featuring “sticker” regions connected by flexible “linkers”. While linkers facilitate many interactions, an understudied question is how the length of linkers influences condensation via an interplay with other molecular length scales. We investigate this in the algal pyrenoid, a condensate that enhances photosynthesis in Chlamydomonas reinhardtii, focusing on the rigid enzyme Rubisco and its flexible partner EPYC1. Our simulations and theory reveal that halving EPYC1 linker lengths decreases critical concentrations by tenfold due to a sensitive molecular “fit” between EPYC1 and Rubisco. We find an inverse relationship between this fit and their phase separation tendency, with natural Rubisco sticker locations optimizing this process. Additionally, we study how Rubisco-EPYC1 condensates wet membranes, which is necessary for proper pyrenoid function, highlighting how evolution fine-tunes protein phase separation through molecular length scales.

Registration to attend virtually is required. Please register here.

Presenting on “Revealing the Principles Behind Biomolecular Condensate Formation in Algal Pyrenoids”.

Trevor GrandPre, PhD, Schmidt Science Fellow, Princeton Center for Theoretical Science Fellow, Center for the Physics of Biological Function Fellow, Future Faculty in the Physical Sciences Fellow at Princeton University will speak on Thursday, September 12, 2024 at 10:00 am in Whitaker 218.

Abstract: Biomolecular condensates are membraneless organelles formed through the phase separation of macromolecules, featuring “sticker” regions connected by flexible “linkers”. While linkers facilitate many interactions, an understudied question is how the length of linkers influences condensation via an interplay with other molecular length scales. We investigate this in the algal pyrenoid, a condensate that enhances photosynthesis in Chlamydomonas reinhardtii, focusing on the rigid enzyme Rubisco and its flexible partner EPYC1. Our simulations and theory reveal that halving EPYC1 linker lengths decreases critical concentrations by tenfold due to a sensitive molecular “fit” between EPYC1 and Rubisco. We find an inverse relationship between this fit and their phase separation tendency, with natural Rubisco sticker locations optimizing this process. Additionally, we study how Rubisco-EPYC1 condensates wet membranes, which is necessary for proper pyrenoid function, highlighting how evolution fine-tunes protein phase separation through molecular length scales.

Registration to attend virtually is required. Please register here.