Fusion of protein aggregates facilitates asymmetric damage segregation.

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. W...

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Autores principales: Miguel Coelho, Steven J Lade, Simon Alberti, Thilo Gross, Iva M Tolić
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Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2014
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Acceso en línea:https://doaj.org/article/991e0c3fd5474dab9fbd13522abee3be
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spelling oai:doaj.org-article:991e0c3fd5474dab9fbd13522abee3be2021-11-11T05:37:08ZFusion of protein aggregates facilitates asymmetric damage segregation.1544-91731545-788510.1371/journal.pbio.1001886https://doaj.org/article/991e0c3fd5474dab9fbd13522abee3be2014-06-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24936793/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Asymmetric 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.Miguel CoelhoSteven J LadeSimon AlbertiThilo GrossIva M TolićPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 12, Iss 6, p e1001886 (2014)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Miguel Coelho
Steven J Lade
Simon Alberti
Thilo Gross
Iva M Tolić
Fusion of protein aggregates facilitates asymmetric damage segregation.
description 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.
format article
author Miguel Coelho
Steven J Lade
Simon Alberti
Thilo Gross
Iva M Tolić
author_facet Miguel Coelho
Steven J Lade
Simon Alberti
Thilo Gross
Iva M Tolić
author_sort Miguel Coelho
title Fusion of protein aggregates facilitates asymmetric damage segregation.
title_short Fusion of protein aggregates facilitates asymmetric damage segregation.
title_full Fusion of protein aggregates facilitates asymmetric damage segregation.
title_fullStr Fusion of protein aggregates facilitates asymmetric damage segregation.
title_full_unstemmed Fusion of protein aggregates facilitates asymmetric damage segregation.
title_sort fusion of protein aggregates facilitates asymmetric damage segregation.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/991e0c3fd5474dab9fbd13522abee3be
work_keys_str_mv AT miguelcoelho fusionofproteinaggregatesfacilitatesasymmetricdamagesegregation
AT stevenjlade fusionofproteinaggregatesfacilitatesasymmetricdamagesegregation
AT simonalberti fusionofproteinaggregatesfacilitatesasymmetricdamagesegregation
AT thilogross fusionofproteinaggregatesfacilitatesasymmetricdamagesegregation
AT ivamtolic fusionofproteinaggregatesfacilitatesasymmetricdamagesegregation
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