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The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB

Bacterial cell division is mediated by a protein complex known as the divisome. Many protein–protein interactions in the divisome have been characterized. In this report, we analyse the role of the PASTA (Penicillin-binding protein And Serine Threonine kinase Associated) domains of Bacillus subtilis...

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Autores principales: Morales Angeles, Danae, Macia-Valero, Alicia, Bohorquez, Laura C., Scheffers, Dirk-Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Microbiology Society 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7654742/
https://www.ncbi.nlm.nih.gov/pubmed/32749956
http://dx.doi.org/10.1099/mic.0.000957
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author Morales Angeles, Danae
Macia-Valero, Alicia
Bohorquez, Laura C.
Scheffers, Dirk-Jan
author_facet Morales Angeles, Danae
Macia-Valero, Alicia
Bohorquez, Laura C.
Scheffers, Dirk-Jan
author_sort Morales Angeles, Danae
collection PubMed
description Bacterial cell division is mediated by a protein complex known as the divisome. Many protein–protein interactions in the divisome have been characterized. In this report, we analyse the role of the PASTA (Penicillin-binding protein And Serine Threonine kinase Associated) domains of Bacillus subtilis PBP2B. PBP2B itself is essential and cannot be deleted, but removing the PBP2B PASTA domains results in impaired cell division and a heat-sensitive phenotype. This resembles the deletion of divIB, a known interaction partner of PBP2B. Bacterial two-hybrid and co-immunoprecipitation analyses show that the interaction between PBP2B and DivIB is weakened when the PBP2B PASTA domains are removed. Combined, our results show that the PBP2B PASTA domains are required to strengthen the interaction between PBP2B and DivIB.
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spelling pubmed-76547422020-11-12 The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB Morales Angeles, Danae Macia-Valero, Alicia Bohorquez, Laura C. Scheffers, Dirk-Jan Microbiology (Reading) Research Article Bacterial cell division is mediated by a protein complex known as the divisome. Many protein–protein interactions in the divisome have been characterized. In this report, we analyse the role of the PASTA (Penicillin-binding protein And Serine Threonine kinase Associated) domains of Bacillus subtilis PBP2B. PBP2B itself is essential and cannot be deleted, but removing the PBP2B PASTA domains results in impaired cell division and a heat-sensitive phenotype. This resembles the deletion of divIB, a known interaction partner of PBP2B. Bacterial two-hybrid and co-immunoprecipitation analyses show that the interaction between PBP2B and DivIB is weakened when the PBP2B PASTA domains are removed. Combined, our results show that the PBP2B PASTA domains are required to strengthen the interaction between PBP2B and DivIB. Microbiology Society 2020-09 2020-08-04 /pmc/articles/PMC7654742/ /pubmed/32749956 http://dx.doi.org/10.1099/mic.0.000957 Text en © 2020 The Authors http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution NonCommercial License.
spellingShingle Research Article
Morales Angeles, Danae
Macia-Valero, Alicia
Bohorquez, Laura C.
Scheffers, Dirk-Jan
The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title_full The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title_fullStr The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title_full_unstemmed The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title_short The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB
title_sort pasta domains of bacillus subtilis pbp2b strengthen the interaction of pbp2b with divib
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7654742/
https://www.ncbi.nlm.nih.gov/pubmed/32749956
http://dx.doi.org/10.1099/mic.0.000957
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