Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli

Research output: Contribution to journalArticlepeer-review

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Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. / van der Ploeg, René; Verheul, Jolanda; Vischer, Norbert O E; Alexeeva, Svetlana; Hoogendoorn, Eelco; Postma, Marten; Banzhaf, Manuel; Vollmer, Waldemar; den Blaauwen, Tanneke.

In: Molecular Microbiology, Vol. 87, No. 5, 03.2013, p. 1074-87.

Research output: Contribution to journalArticlepeer-review

Harvard

van der Ploeg, R, Verheul, J, Vischer, NOE, Alexeeva, S, Hoogendoorn, E, Postma, M, Banzhaf, M, Vollmer, W & den Blaauwen, T 2013, 'Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli', Molecular Microbiology, vol. 87, no. 5, pp. 1074-87. https://doi.org/10.1111/mmi.12150

APA

van der Ploeg, R., Verheul, J., Vischer, N. O. E., Alexeeva, S., Hoogendoorn, E., Postma, M., Banzhaf, M., Vollmer, W., & den Blaauwen, T. (2013). Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. Molecular Microbiology, 87(5), 1074-87. https://doi.org/10.1111/mmi.12150

Vancouver

Author

van der Ploeg, René ; Verheul, Jolanda ; Vischer, Norbert O E ; Alexeeva, Svetlana ; Hoogendoorn, Eelco ; Postma, Marten ; Banzhaf, Manuel ; Vollmer, Waldemar ; den Blaauwen, Tanneke. / Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. In: Molecular Microbiology. 2013 ; Vol. 87, No. 5. pp. 1074-87.

Bibtex

@article{27e692880a3b469680149eb16c20e9b4,
title = "Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli",
abstract = "The rod-shaped bacterium Escherichia coli grows by insertion of peptidoglycan into the lateral wall during cell elongation and synthesis of new poles during cell division. The monofunctional transpeptidases PBP2 and PBP3 are part of specialized protein complexes called elongasome and divisome, respectively, which catalyse peptidoglycan extension and maturation. Endogenous immunolabelled PBP2 localized in the cylindrical part of the cell as well as transiently at midcell. Using the novel image analysis tool Coli-Inspector to analyse protein localization as function of the bacterial cell age, we compared PBP2 localization with that of other E. coli cell elongation and division proteins including PBP3. Interestingly, the midcell localization of the two transpeptidases overlaps in time during the early period of divisome maturation. F{\"o}rsters Resonance Energy Transfer (FRET) experiments revealed an interaction between PBP2 and PBP3 when both are present at midcell. A decrease in the midcell diameter is visible after 40% of the division cycle indicating that the onset of new cell pole synthesis starts much earlier than previously identified by visual inspection. The data support a new model of the division cycle in which the elongasome and divisome interact to prepare for cell division.",
keywords = "Cell Division, Escherichia coli, Escherichia coli Proteins, Organelles, Peptidyl Transferases, Protein Binding, Protein Transport, Journal Article, Research Support, Non-U.S. Gov't",
author = "{van der Ploeg}, Ren{\'e} and Jolanda Verheul and Vischer, {Norbert O E} and Svetlana Alexeeva and Eelco Hoogendoorn and Marten Postma and Manuel Banzhaf and Waldemar Vollmer and {den Blaauwen}, Tanneke",
note = "{\textcopyright} 2013 Blackwell Publishing Ltd.",
year = "2013",
month = mar,
doi = "10.1111/mmi.12150",
language = "English",
volume = "87",
pages = "1074--87",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley",
number = "5",

}

RIS

TY - JOUR

T1 - Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli

AU - van der Ploeg, René

AU - Verheul, Jolanda

AU - Vischer, Norbert O E

AU - Alexeeva, Svetlana

AU - Hoogendoorn, Eelco

AU - Postma, Marten

AU - Banzhaf, Manuel

AU - Vollmer, Waldemar

AU - den Blaauwen, Tanneke

N1 - © 2013 Blackwell Publishing Ltd.

PY - 2013/3

Y1 - 2013/3

N2 - The rod-shaped bacterium Escherichia coli grows by insertion of peptidoglycan into the lateral wall during cell elongation and synthesis of new poles during cell division. The monofunctional transpeptidases PBP2 and PBP3 are part of specialized protein complexes called elongasome and divisome, respectively, which catalyse peptidoglycan extension and maturation. Endogenous immunolabelled PBP2 localized in the cylindrical part of the cell as well as transiently at midcell. Using the novel image analysis tool Coli-Inspector to analyse protein localization as function of the bacterial cell age, we compared PBP2 localization with that of other E. coli cell elongation and division proteins including PBP3. Interestingly, the midcell localization of the two transpeptidases overlaps in time during the early period of divisome maturation. Försters Resonance Energy Transfer (FRET) experiments revealed an interaction between PBP2 and PBP3 when both are present at midcell. A decrease in the midcell diameter is visible after 40% of the division cycle indicating that the onset of new cell pole synthesis starts much earlier than previously identified by visual inspection. The data support a new model of the division cycle in which the elongasome and divisome interact to prepare for cell division.

AB - The rod-shaped bacterium Escherichia coli grows by insertion of peptidoglycan into the lateral wall during cell elongation and synthesis of new poles during cell division. The monofunctional transpeptidases PBP2 and PBP3 are part of specialized protein complexes called elongasome and divisome, respectively, which catalyse peptidoglycan extension and maturation. Endogenous immunolabelled PBP2 localized in the cylindrical part of the cell as well as transiently at midcell. Using the novel image analysis tool Coli-Inspector to analyse protein localization as function of the bacterial cell age, we compared PBP2 localization with that of other E. coli cell elongation and division proteins including PBP3. Interestingly, the midcell localization of the two transpeptidases overlaps in time during the early period of divisome maturation. Försters Resonance Energy Transfer (FRET) experiments revealed an interaction between PBP2 and PBP3 when both are present at midcell. A decrease in the midcell diameter is visible after 40% of the division cycle indicating that the onset of new cell pole synthesis starts much earlier than previously identified by visual inspection. The data support a new model of the division cycle in which the elongasome and divisome interact to prepare for cell division.

KW - Cell Division

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Organelles

KW - Peptidyl Transferases

KW - Protein Binding

KW - Protein Transport

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1111/mmi.12150

DO - 10.1111/mmi.12150

M3 - Article

C2 - 23387922

VL - 87

SP - 1074

EP - 1087

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 5

ER -