20 min listen
Adaptive preservation of orphan ribosomal proteins in chaperone-stirred condensates
Adaptive preservation of orphan ribosomal proteins in chaperone-stirred condensates
ratings:
Length:
20 minutes
Released:
Nov 10, 2022
Format:
Podcast episode
Description
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2022.11.09.515856v1?rss=1
Authors: Ali, A., Garde, R., Schaffer, O. C., Bard, J. A. M., Husain, K., Keyport Kik, S., Davis, K. A., Luengo-Woods, S., Drummond, D. A., Squires, A. H., Pincus, D.
Abstract:
Ribosome biogenesis is among the most resource-intensive cellular processes, with ribosomal proteins accounting for up to half of all newly synthesized proteins in eukaryotic cells. During stress, cells shut down ribosome biogenesis in part by halting rRNA synthesis, potentially leading to massive accumulation of aggregation-prone 'orphan' ribosomal proteins (oRPs). Here we show that during heat shock in yeast and human cells, oRPs accumulate as reversible condensates at the nucleolar periphery recognized by the Hsp70 co-chaperone Sis1/DnaJB6. oRP condensates are liquid-like in cell-free lysate but solidify upon depletion of Sis1 or inhibition of Hsp70. When cells recover from heat shock, oRP condensates disperse in a Sis1-dependent manner, and their ribosomal protein constituents are incorporated into functional ribosomes in the cytosol, enabling cells to efficiently resume growth.
Copy rights belong to original authors. Visit the link for more info
Podcast created by Paper Player, LLC
http://biorxiv.org/cgi/content/short/2022.11.09.515856v1?rss=1
Authors: Ali, A., Garde, R., Schaffer, O. C., Bard, J. A. M., Husain, K., Keyport Kik, S., Davis, K. A., Luengo-Woods, S., Drummond, D. A., Squires, A. H., Pincus, D.
Abstract:
Ribosome biogenesis is among the most resource-intensive cellular processes, with ribosomal proteins accounting for up to half of all newly synthesized proteins in eukaryotic cells. During stress, cells shut down ribosome biogenesis in part by halting rRNA synthesis, potentially leading to massive accumulation of aggregation-prone 'orphan' ribosomal proteins (oRPs). Here we show that during heat shock in yeast and human cells, oRPs accumulate as reversible condensates at the nucleolar periphery recognized by the Hsp70 co-chaperone Sis1/DnaJB6. oRP condensates are liquid-like in cell-free lysate but solidify upon depletion of Sis1 or inhibition of Hsp70. When cells recover from heat shock, oRP condensates disperse in a Sis1-dependent manner, and their ribosomal protein constituents are incorporated into functional ribosomes in the cytosol, enabling cells to efficiently resume growth.
Copy rights belong to original authors. Visit the link for more info
Podcast created by Paper Player, LLC
Released:
Nov 10, 2022
Format:
Podcast episode
Titles in the series (100)
FBXL4 deficiency promotes mitophagy by elevating NIX. by PaperPlayer biorxiv cell biology