TY - JOUR
T1 - Regulation of peptidoglycan synthesis by outer-membrane proteins
AU - Typas, Athanasios
AU - Banzhaf, Manuel
AU - van den Berg van Saparoea, Bart
AU - Verheul, Jolanda
AU - Biboy, Jacob
AU - Nichols, Robert J
AU - Zietek, Matylda
AU - Beilharz, Katrin
AU - Kannenberg, Kai
AU - von Rechenberg, Moritz
AU - Breukink, Eefjan
AU - den Blaauwen, Tanneke
AU - Gross, Carol A
AU - Vollmer, Waldemar
N1 - Copyright © 2010 Elsevier Inc. All rights reserved.
PY - 2010/12/23
Y1 - 2010/12/23
N2 - Growth of the mesh-like peptidoglycan (PG) sacculus located between the bacterial inner and outer membranes (OM) is tightly regulated to ensure cellular integrity, maintain cell shape, and orchestrate division. Cytoskeletal elements direct placement and activity of PG synthases from inside the cell, but precise spatiotemporal control over this process is poorly understood. We demonstrate that PG synthases are also controlled from outside of the sacculus. Two OM lipoproteins, LpoA and LpoB, are essential for the function, respectively, of PBP1A and PBP1B, the major E. coli bifunctional PG synthases. Each Lpo protein binds specifically to its cognate PBP and stimulates its transpeptidase activity, thereby facilitating attachment of new PG to the sacculus. LpoB shows partial septal localization, and our data suggest that the LpoB-PBP1B complex contributes to OM constriction during cell division. LpoA/LpoB and their PBP-docking regions are restricted to γ-proteobacteria, providing models for niche-specific regulation of sacculus growth.
AB - Growth of the mesh-like peptidoglycan (PG) sacculus located between the bacterial inner and outer membranes (OM) is tightly regulated to ensure cellular integrity, maintain cell shape, and orchestrate division. Cytoskeletal elements direct placement and activity of PG synthases from inside the cell, but precise spatiotemporal control over this process is poorly understood. We demonstrate that PG synthases are also controlled from outside of the sacculus. Two OM lipoproteins, LpoA and LpoB, are essential for the function, respectively, of PBP1A and PBP1B, the major E. coli bifunctional PG synthases. Each Lpo protein binds specifically to its cognate PBP and stimulates its transpeptidase activity, thereby facilitating attachment of new PG to the sacculus. LpoB shows partial septal localization, and our data suggest that the LpoB-PBP1B complex contributes to OM constriction during cell division. LpoA/LpoB and their PBP-docking regions are restricted to γ-proteobacteria, providing models for niche-specific regulation of sacculus growth.
KW - Bacterial Outer Membrane Proteins
KW - Cell Division
KW - Cell Wall
KW - Escherichia coli
KW - Escherichia coli Proteins
KW - Lipoproteins
KW - Penicillin-Binding Proteins
KW - Peptidoglycan
KW - Peptidoglycan Glycosyltransferase
KW - Protein Interaction Domains and Motifs
KW - Journal Article
KW - Research Support, N.I.H., Extramural
KW - Research Support, Non-U.S. Gov't
U2 - 10.1016/j.cell.2010.11.038
DO - 10.1016/j.cell.2010.11.038
M3 - Article
C2 - 21183073
SN - 0092-8674
VL - 143
SP - 1097
EP - 1109
JO - Cell
JF - Cell
IS - 7
ER -