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A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1
Subcellular targeting of proteins is essential to orchestrate cytokinesis in eukaryotic cells. During cell division of Ustilago maydis, for example, chitinases must be specifically targeted to the fragmentation zone at the site of cell division to degrade remnant chitin and thus separate mother and...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7358432/ https://www.ncbi.nlm.nih.gov/pubmed/32733418 http://dx.doi.org/10.3389/fmicb.2020.01529 |
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author | Reindl, Michèle Stock, Janpeter Hussnaetter, Kai P. Genc, Aycin Brachmann, Andreas Schipper, Kerstin |
author_facet | Reindl, Michèle Stock, Janpeter Hussnaetter, Kai P. Genc, Aycin Brachmann, Andreas Schipper, Kerstin |
author_sort | Reindl, Michèle |
collection | PubMed |
description | Subcellular targeting of proteins is essential to orchestrate cytokinesis in eukaryotic cells. During cell division of Ustilago maydis, for example, chitinases must be specifically targeted to the fragmentation zone at the site of cell division to degrade remnant chitin and thus separate mother and daughter cells. Chitinase Cts1 is exported to this location via an unconventional secretion pathway putatively operating in a lock-type manner. The underlying mechanism is largely unexplored. Here, we applied a forward genetic screen based on UV mutagenesis to identify components essential for Cts1 export. The screen revealed a novel factor termed Jps1 lacking known protein domains. Deletion of the corresponding gene confirmed its essential role for Cts1 secretion. Localization studies demonstrated that Jps1 colocalizes with Cts1 in the fragmentation zone of dividing yeast cells. While loss of Jps1 leads to exclusion of Cts1 from the fragmentation zone and strongly reduced unconventional secretion, deletion of the chitinase does not disturb Jps1 localization. Yeast-two hybrid experiments indicate that the two proteins might interact. In essence, we identified a novel component of unconventional secretion that functions in the fragmentation zone to enable export of Cts1. We hypothesize that Jps1 acts as an anchoring factor for Cts1. |
format | Online Article Text |
id | pubmed-7358432 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73584322020-07-29 A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 Reindl, Michèle Stock, Janpeter Hussnaetter, Kai P. Genc, Aycin Brachmann, Andreas Schipper, Kerstin Front Microbiol Microbiology Subcellular targeting of proteins is essential to orchestrate cytokinesis in eukaryotic cells. During cell division of Ustilago maydis, for example, chitinases must be specifically targeted to the fragmentation zone at the site of cell division to degrade remnant chitin and thus separate mother and daughter cells. Chitinase Cts1 is exported to this location via an unconventional secretion pathway putatively operating in a lock-type manner. The underlying mechanism is largely unexplored. Here, we applied a forward genetic screen based on UV mutagenesis to identify components essential for Cts1 export. The screen revealed a novel factor termed Jps1 lacking known protein domains. Deletion of the corresponding gene confirmed its essential role for Cts1 secretion. Localization studies demonstrated that Jps1 colocalizes with Cts1 in the fragmentation zone of dividing yeast cells. While loss of Jps1 leads to exclusion of Cts1 from the fragmentation zone and strongly reduced unconventional secretion, deletion of the chitinase does not disturb Jps1 localization. Yeast-two hybrid experiments indicate that the two proteins might interact. In essence, we identified a novel component of unconventional secretion that functions in the fragmentation zone to enable export of Cts1. We hypothesize that Jps1 acts as an anchoring factor for Cts1. Frontiers Media S.A. 2020-07-07 /pmc/articles/PMC7358432/ /pubmed/32733418 http://dx.doi.org/10.3389/fmicb.2020.01529 Text en Copyright © 2020 Reindl, Stock, Hussnaetter, Genc, Brachmann and Schipper. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Reindl, Michèle Stock, Janpeter Hussnaetter, Kai P. Genc, Aycin Brachmann, Andreas Schipper, Kerstin A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title | A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title_full | A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title_fullStr | A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title_full_unstemmed | A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title_short | A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1 |
title_sort | novel factor essential for unconventional secretion of chitinase cts1 |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7358432/ https://www.ncbi.nlm.nih.gov/pubmed/32733418 http://dx.doi.org/10.3389/fmicb.2020.01529 |
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