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SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
During sporulation in Bacillus subtilis, a group of mother cell‐specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coa...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282716/ https://www.ncbi.nlm.nih.gov/pubmed/30168214 http://dx.doi.org/10.1111/mmi.14116 |
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author | Nunes, Filipa Fernandes, Catarina Freitas, Carolina Marini, Eleonora Serrano, Mónica Moran, Charles P. Eichenberger, Patrick Henriques, Adriano O. |
author_facet | Nunes, Filipa Fernandes, Catarina Freitas, Carolina Marini, Eleonora Serrano, Mónica Moran, Charles P. Eichenberger, Patrick Henriques, Adriano O. |
author_sort | Nunes, Filipa |
collection | PubMed |
description | During sporulation in Bacillus subtilis, a group of mother cell‐specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coat layers. Targeting of coat proteins to the developing spore is followed by encasement. Encasement by SafA and CotE requires E, a region of 11 amino acids in the encasement protein SpoVID, with which CotE interacts directly. Here, we identified two single alanine substitutions in E that prevent binding of SafA, but not of CotE, to SpoVID, and block encasement. The substitutions result in the accumulation of SafA, CotE and their dependent proteins at the mother cell proximal spore pole, phenocopying a spoVID null mutant and suggesting that mislocalized SafA acts as an attractor for the rest of the coat. The requirement for E in SafA binding is bypassed by a peptide with the sequence of E provided in trans. We suggest that E allows binding of SafA to a second region in SpoVID, enabling CotE to interact with E and SpoVID to function as a non‐competitive hub during spore encasement. |
format | Online Article Text |
id | pubmed-6282716 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-62827162018-12-11 SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis Nunes, Filipa Fernandes, Catarina Freitas, Carolina Marini, Eleonora Serrano, Mónica Moran, Charles P. Eichenberger, Patrick Henriques, Adriano O. Mol Microbiol Research Articles During sporulation in Bacillus subtilis, a group of mother cell‐specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coat layers. Targeting of coat proteins to the developing spore is followed by encasement. Encasement by SafA and CotE requires E, a region of 11 amino acids in the encasement protein SpoVID, with which CotE interacts directly. Here, we identified two single alanine substitutions in E that prevent binding of SafA, but not of CotE, to SpoVID, and block encasement. The substitutions result in the accumulation of SafA, CotE and their dependent proteins at the mother cell proximal spore pole, phenocopying a spoVID null mutant and suggesting that mislocalized SafA acts as an attractor for the rest of the coat. The requirement for E in SafA binding is bypassed by a peptide with the sequence of E provided in trans. We suggest that E allows binding of SafA to a second region in SpoVID, enabling CotE to interact with E and SpoVID to function as a non‐competitive hub during spore encasement. John Wiley and Sons Inc. 2018-10-18 2018-11 /pmc/articles/PMC6282716/ /pubmed/30168214 http://dx.doi.org/10.1111/mmi.14116 Text en © 2018 The Authors. Molecular Microbiology Published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Nunes, Filipa Fernandes, Catarina Freitas, Carolina Marini, Eleonora Serrano, Mónica Moran, Charles P. Eichenberger, Patrick Henriques, Adriano O. SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis |
title | SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
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title_full | SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
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title_fullStr | SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
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title_full_unstemmed | SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
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title_short | SpoVID functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in Bacillus subtilis
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title_sort | spovid functions as a non‐competitive hub that connects the modules for assembly of the inner and outer spore coat layers in bacillus subtilis |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282716/ https://www.ncbi.nlm.nih.gov/pubmed/30168214 http://dx.doi.org/10.1111/mmi.14116 |
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