Janhavi Kohle (PhD, cell and developmental biology, '22) Scientists have long known about the existence of unstructured protein regions, but their perspectives on the role these regions play is shifting, said first author Janhavi Kolhe (PhD, cell and developmental biology, ’22). Intriguingly, the lab found that Hsp90 recognizes intrinsically disordered regions within target proteins, which serve as hubs for chaperone-binding. The Freeman Lab’s research, published in Molecular Cell, showed that Hsp90 associated with roughly one-fifth of the yeast proteome using its three structural domains. Thanks to their new approach of crosslinking cell proteins directly to their interaction partners, Professor Brian Freeman's lab in the Department of Cell & Developmental Biology has identified protein interaction features of the molecular chaperone called Hsp90.
By doing so, molecular chaperones ensure proteins are properly created and utilized before they’re dismantled at the ends of their lifespans. Molecular chaperones serve to support the health of all proteins, including the folding of nascent protein chains. Through a new approach of cross-linking cell proteins directly to a protein of interest, researchers at the University of Illinois Urbana-Champaign’s School of Molecular & Cellular Biology have distinguished new patterns of cell interactions with a molecular chaperone.
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