Fusion of protein aggregates facilitates asymmetric damage segregation.

Bibliographic Details
Title: Fusion of protein aggregates facilitates asymmetric damage segregation.
Authors: Miguel Coelho, Steven J Lade, Simon Alberti, Thilo Gross, Iva M Tolić
Source: PLoS Biology, Vol 12, Iss 6, p e1001886 (2014)
Publisher Information: Public Library of Science (PLoS), 2014.
Publication Year: 2014
Collection: LCC:Biology (General)
Subject Terms: Biology (General), QH301-705.5
More Details: Asymmetric segregation of damaged proteins at cell division generates a cell that retains damage and a clean cell that supports population survival. In cells that divide asymmetrically, such as Saccharomyces cerevisiae, segregation of damaged proteins is achieved by retention and active transport. We have previously shown that in the symmetrically dividing Schizosaccharomyces pombe there is a transition between symmetric and asymmetric segregation of damaged proteins. Yet how this transition and generation of damage-free cells are achieved remained unknown. Here, by combining in vivo imaging of Hsp104-associated aggregates, a form of damage, with mathematical modeling, we find that fusion of protein aggregates facilitates asymmetric segregation. Our model predicts that, after stress, the increased number of aggregates fuse into a single large unit, which is inherited asymmetrically by one daughter cell, whereas the other one is born clean. We experimentally confirmed that fusion increases segregation asymmetry, for a range of stresses, and identified Hsp16 as a fusion factor. Our work shows that fusion of protein aggregates promotes the formation of damage-free cells. Fusion of cellular factors may represent a general mechanism for their asymmetric segregation at division.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1544-9173
1545-7885
Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24936793/?tool=EBI; https://doaj.org/toc/1544-9173; https://doaj.org/toc/1545-7885
DOI: 10.1371/journal.pbio.1001886
Access URL: https://doaj.org/article/991e0c3fd5474dab9fbd13522abee3be
Accession Number: edsdoj.991e0c3fd5474dab9fbd13522abee3be
Database: Directory of Open Access Journals
More Details
ISSN:15449173
15457885
DOI:10.1371/journal.pbio.1001886
Published in:PLoS Biology
Language:English