Inhibition of penicillin-binding protein 3 of Escherichia coli K-12. Effects upon growth, viability and outer membrane barrier function

1985 ◽  
Vol 16 (3) ◽  
pp. 287-296 ◽  
Author(s):  
Nigel A. C. Curtis ◽  
Rosemary L. Eisenstadt ◽  
Kath A. Turner ◽  
Anthony J. White
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Barrier Function ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Membrane Barrier ◽  
K 12

scholarly journals Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli

2014 ◽  
Vol 9 (1) ◽  
pp. 123-127 ◽  
Author(s):  
Nicolas L. Jean ◽  
Catherine M. Bougault ◽  
Alexander J. F. Egan ◽  
Waldemar Vollmer ◽  
Jean-Pierre Simorre
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Nmr Assignment ◽  
Binding Protein ◽  
Solution Nmr ◽  
Penicillin Binding Protein ◽  
Protein Activator

scholarly journals Mutations in enterobacterial common antigen biosynthesis restore outer membrane barrier function in Escherichia coli tol-pal mutants

2018 ◽  
Author(s):  
Xiang’Er Jiang ◽  
Wee Boon Tan ◽  
Rahul Shrivastava ◽  
Deborah Chwee San Seow ◽  
Swaine Lin Chen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Barrier Function ◽  
Lipid Homeostasis ◽  
Common Antigen ◽  
Potential Mechanism ◽  
External Threats ◽  
Enterobacterial Common Antigen ◽  
Lipid Species ◽  
Membrane Barrier

SummaryThe outer membrane (OM) is an essential component of the Gram-negative bacterial envelope that protects cells against external threats. To maintain a functional OM, cells require distinct mechanisms to ensure balance of proteins and lipids in the membrane. Mutations in OM biogenesis and/or homeostasis pathways often result in permeability defects, but how molecular changes in the OM affect barrier function is unclear. Here, we seek potential mechanism(s) that can alleviate permeability defects in Escherichia coli cells lacking the Tol-Pal complex, which accumulate excess PLs in the OM. We identify mutations in enterobacterial common antigen (ECA) biosynthesis that re-establish OM barrier function against large hydrophilic molecules, yet did not restore lipid homeostasis. Furthermore, we demonstrate that build-up of biosynthetic intermediates, but not loss of ECA itself, contributes to the rescue. This suppression of OM phenotypes is unrelated to known effects that accumulation of ECA intermediates have on the cell wall. Finally, we reveal that an unusual diacylglycerol pyrophosphoryl-linked lipid species also accumulates in ECA mutants, and might play a role in the rescue phenotype. Our work provides insights into how OM barrier function can be restored independent of lipid homeostasis, and highlights previously unappreciated effects of ECA-related species in OM biology.

scholarly journals Further studies on rod A mutant: A round morphological mutant of Escherichia coli K-12 with wild-type penicillin-binding protein 2.

1980 ◽  
Vol 44 (12) ◽  
pp. 2937-2941 ◽  
Author(s):  
Hiroshi MATSUZAWA ◽  
Sadamitsu ASOH ◽  
Takahisa OHTA ◽  
Shigeo TAMAKI ◽  
Michio MATSUHASHI
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Morphological Mutant ◽  
K 12

scholarly journals Mutations in enterobacterial common antigen biosynthesis restore outer membrane barrier function in Escherichia coli tol‐pal mutants

2020 ◽  
Vol 114 (6) ◽  
pp. 991-1005
Author(s):  
Xiang’Er Jiang ◽  
Wee Boon Tan ◽  
Rahul Shrivastava ◽  
Deborah Chwee San Seow ◽  
Swaine Lin Chen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Barrier Function ◽  
Common Antigen ◽  
Enterobacterial Common Antigen ◽  
Membrane Barrier

In vitro peptidoglycan polymerization catalysed by penicillin binding protein 1b of Escherichia coli K-12

FEBS Letters ◽  
1980 ◽  
Vol 110 (2) ◽  
pp. 245-249 ◽  
Author(s):  
Hideho Suzuki ◽  
Yveline Van Heijenoort ◽  
Toshihide Tamura ◽  
Junzo Mizoguchi ◽  
Yukinori Hirota ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
K 12
Sign in / Sign up

Export Citation Format

Share Document