Cooperativity of peptidoglycan synthases active in bacterial cell elongation

Research output: Contribution to journalArticlepeer-review

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Cooperativity of peptidoglycan synthases active in bacterial cell elongation. / Banzhaf, Manuel; van den Berg van Saparoea, Bart; Terrak, Mohammed; Fraipont, Claudine; Egan, Alexander; Philippe, Jules; Zapun, André; Breukink, Eefjan; Nguyen-Distèche, Martine; den Blaauwen, Tanneke; Vollmer, Waldemar.

In: Molecular Microbiology, Vol. 85, No. 1, 07.2012, p. 179-94.

Research output: Contribution to journalArticlepeer-review

Harvard

Banzhaf, M, van den Berg van Saparoea, B, Terrak, M, Fraipont, C, Egan, A, Philippe, J, Zapun, A, Breukink, E, Nguyen-Distèche, M, den Blaauwen, T & Vollmer, W 2012, 'Cooperativity of peptidoglycan synthases active in bacterial cell elongation', Molecular Microbiology, vol. 85, no. 1, pp. 179-94. https://doi.org/10.1111/j.1365-2958.2012.08103.x

APA

Banzhaf, M., van den Berg van Saparoea, B., Terrak, M., Fraipont, C., Egan, A., Philippe, J., Zapun, A., Breukink, E., Nguyen-Distèche, M., den Blaauwen, T., & Vollmer, W. (2012). Cooperativity of peptidoglycan synthases active in bacterial cell elongation. Molecular Microbiology, 85(1), 179-94. https://doi.org/10.1111/j.1365-2958.2012.08103.x

Vancouver

Banzhaf M, van den Berg van Saparoea B, Terrak M, Fraipont C, Egan A, Philippe J et al. Cooperativity of peptidoglycan synthases active in bacterial cell elongation. Molecular Microbiology. 2012 Jul;85(1):179-94. https://doi.org/10.1111/j.1365-2958.2012.08103.x

Author

Banzhaf, Manuel ; van den Berg van Saparoea, Bart ; Terrak, Mohammed ; Fraipont, Claudine ; Egan, Alexander ; Philippe, Jules ; Zapun, André ; Breukink, Eefjan ; Nguyen-Distèche, Martine ; den Blaauwen, Tanneke ; Vollmer, Waldemar. / Cooperativity of peptidoglycan synthases active in bacterial cell elongation. In: Molecular Microbiology. 2012 ; Vol. 85, No. 1. pp. 179-94.

Bibtex

@article{1c8fd4539e8c459c8cf2f960d9fab963,
title = "Cooperativity of peptidoglycan synthases active in bacterial cell elongation",
abstract = "Growth of the bacterial cell wall peptidoglycan sacculus requires the co-ordinated activities of peptidoglycan synthases, hydrolases and cell morphogenesis proteins, but the details of these interactions are largely unknown. We now show that the Escherichia coli peptidoglycan glycosyltrasferase-transpeptidase PBP1A interacts with the cell elongation-specific transpeptidase PBP2 in vitro and in the cell. Cells lacking PBP1A are thinner and initiate cell division later in the cell cycle. PBP1A localizes mainly to the cylindrical wall of the cell, supporting its role in cell elongation. Our in vitro peptidoglycan synthesis assays provide novel insights into the cooperativity of peptidoglycan synthases with different activities. PBP2 stimulates the glycosyltransferase activity of PBP1A, and PBP1A and PBP2 cooperate to attach newly synthesized peptidoglycan to sacculi. PBP2 has peptidoglycan transpeptidase activity in the presence of active PBP1A. Our data also provide a possible explanation for the depletion of lipid II precursors in penicillin-treated cells.",
keywords = "Cell Wall, Escherichia coli, Escherichia coli Proteins, Penicillin-Binding Proteins, Peptidoglycan, Peptidoglycan Glycosyltransferase, Journal Article, Research Support, Non-U.S. Gov't",
author = "Manuel Banzhaf and {van den Berg van Saparoea}, Bart and Mohammed Terrak and Claudine Fraipont and Alexander Egan and Jules Philippe and Andr{\'e} Zapun and Eefjan Breukink and Martine Nguyen-Dist{\`e}che and {den Blaauwen}, Tanneke and Waldemar Vollmer",
note = "{\textcopyright} 2012 Blackwell Publishing Ltd.",
year = "2012",
month = jul,
doi = "10.1111/j.1365-2958.2012.08103.x",
language = "English",
volume = "85",
pages = "179--94",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley",
number = "1",

}

RIS

TY - JOUR

T1 - Cooperativity of peptidoglycan synthases active in bacterial cell elongation

AU - Banzhaf, Manuel

AU - van den Berg van Saparoea, Bart

AU - Terrak, Mohammed

AU - Fraipont, Claudine

AU - Egan, Alexander

AU - Philippe, Jules

AU - Zapun, André

AU - Breukink, Eefjan

AU - Nguyen-Distèche, Martine

AU - den Blaauwen, Tanneke

AU - Vollmer, Waldemar

N1 - © 2012 Blackwell Publishing Ltd.

PY - 2012/7

Y1 - 2012/7

N2 - Growth of the bacterial cell wall peptidoglycan sacculus requires the co-ordinated activities of peptidoglycan synthases, hydrolases and cell morphogenesis proteins, but the details of these interactions are largely unknown. We now show that the Escherichia coli peptidoglycan glycosyltrasferase-transpeptidase PBP1A interacts with the cell elongation-specific transpeptidase PBP2 in vitro and in the cell. Cells lacking PBP1A are thinner and initiate cell division later in the cell cycle. PBP1A localizes mainly to the cylindrical wall of the cell, supporting its role in cell elongation. Our in vitro peptidoglycan synthesis assays provide novel insights into the cooperativity of peptidoglycan synthases with different activities. PBP2 stimulates the glycosyltransferase activity of PBP1A, and PBP1A and PBP2 cooperate to attach newly synthesized peptidoglycan to sacculi. PBP2 has peptidoglycan transpeptidase activity in the presence of active PBP1A. Our data also provide a possible explanation for the depletion of lipid II precursors in penicillin-treated cells.

AB - Growth of the bacterial cell wall peptidoglycan sacculus requires the co-ordinated activities of peptidoglycan synthases, hydrolases and cell morphogenesis proteins, but the details of these interactions are largely unknown. We now show that the Escherichia coli peptidoglycan glycosyltrasferase-transpeptidase PBP1A interacts with the cell elongation-specific transpeptidase PBP2 in vitro and in the cell. Cells lacking PBP1A are thinner and initiate cell division later in the cell cycle. PBP1A localizes mainly to the cylindrical wall of the cell, supporting its role in cell elongation. Our in vitro peptidoglycan synthesis assays provide novel insights into the cooperativity of peptidoglycan synthases with different activities. PBP2 stimulates the glycosyltransferase activity of PBP1A, and PBP1A and PBP2 cooperate to attach newly synthesized peptidoglycan to sacculi. PBP2 has peptidoglycan transpeptidase activity in the presence of active PBP1A. Our data also provide a possible explanation for the depletion of lipid II precursors in penicillin-treated cells.

KW - Cell Wall

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Penicillin-Binding Proteins

KW - Peptidoglycan

KW - Peptidoglycan Glycosyltransferase

KW - Journal Article

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

U2 - 10.1111/j.1365-2958.2012.08103.x

DO - 10.1111/j.1365-2958.2012.08103.x

M3 - Article

C2 - 22606933

VL - 85

SP - 179

EP - 194

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 1

ER -