Publication

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

Morales Angeles, D., Macia-Valero, A., Bohorquez, L. C. & Scheffers, D-J., 4-Aug-2020, In : Microbiology-Reading. 11 p., mic.0.000957.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Morales Angeles, D., Macia-Valero, A., Bohorquez, L. C., & Scheffers, D-J. (2020). The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB. Microbiology-Reading, [mic.0.000957]. https://doi.org/10.1099/mic.0.000957

Author

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. In: Microbiology-Reading. 2020.

Harvard

Morales Angeles, D, Macia-Valero, A, Bohorquez, LC & Scheffers, D-J 2020, 'The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB', Microbiology-Reading. https://doi.org/10.1099/mic.0.000957

Standard

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.

In: Microbiology-Reading, 04.08.2020.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Morales Angeles D, Macia-Valero A, Bohorquez LC, Scheffers D-J. The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB. Microbiology-Reading. 2020 Aug 4. mic.0.000957. https://doi.org/10.1099/mic.0.000957


BibTeX

@article{ee612f82b411476b87465970bd2b66da,
title = "The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB",
abstract = "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.",
author = "{Morales Angeles}, Danae and Alicia Macia-Valero and Bohorquez, {Laura C} and Dirk-Jan Scheffers",
year = "2020",
month = aug,
day = "4",
doi = "10.1099/mic.0.000957",
language = "English",
journal = "Microbiology-Reading",
issn = "1350-0872",
publisher = "AMER SOC MICROBIOLOGY",

}

RIS

TY - JOUR

T1 - The PASTA domains of Bacillus subtilis PBP2B strengthen the interaction of PBP2B with DivIB

AU - Morales Angeles, Danae

AU - Macia-Valero, Alicia

AU - Bohorquez, Laura C

AU - Scheffers, Dirk-Jan

PY - 2020/8/4

Y1 - 2020/8/4

N2 - 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.

AB - 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.

U2 - 10.1099/mic.0.000957

DO - 10.1099/mic.0.000957

M3 - Article

C2 - 32749956

JO - Microbiology-Reading

JF - Microbiology-Reading

SN - 1350-0872

M1 - mic.0.000957

ER -

ID: 130758473