scholarly journals SOS-Independent Induction of dinB Transcription by β-Lactam-Mediated Inhibition of Cell Wall Synthesis in Escherichia coli

2005 ◽  
Vol 187 (4) ◽  
pp. 1515-1518 ◽  
Author(s):  
Tatiana Pérez-Capilla ◽  
María-Rosario Baquero ◽  
José-María Gómez-Gómez ◽  
Alina Ionel ◽  
Soledad Martín ◽  
...  

ABSTRACT Transcription of the dinB gene, encoding DNA polymerase IV, is induced by the inhibition of cell wall synthesis at different levels. Using the β-lactam antibiotic ceftazidime, a PBP3 inhibitor, as a model, we have shown that this induction is independent of the LexA/RecA regulatory system. Induction of dinB transcription mediated by ceftazidime produces an increase in the reversion of a +1 Lac frameshift mutation.

2004 ◽  
Vol 48 (3) ◽  
pp. 961-969 ◽  
Author(s):  
Astrid Zervosen ◽  
Wei-Ping Lu ◽  
Zhouliang Chen ◽  
Ronald E. White ◽  
Thomas P. Demuth ◽  
...  

ABSTRACT Several non-β-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus MI339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium. The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus, and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 dd-peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 μM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor (Ki = 10 μM) was not influenced by the presence of the substrate.


1999 ◽  
Vol 96 (21) ◽  
pp. 11922-11927 ◽  
Author(s):  
V. L. Gerlach ◽  
L. Aravind ◽  
G. Gotway ◽  
R. A. Schultz ◽  
E. V. Koonin ◽  
...  

2013 ◽  
Vol 41 (9) ◽  
pp. 5104-5114 ◽  
Author(s):  
Amit Sharma ◽  
Jithesh Kottur ◽  
Naveen Narayanan ◽  
Deepak T. Nair

1989 ◽  
Vol 35 (2) ◽  
pp. 318-321 ◽  
Author(s):  
A. Gálvez ◽  
E. Valdivia ◽  
M. Martínez ◽  
M. Maqueda

Peptide antibiotic AS-48 exerts a bactericidal mode of action on exponential cultures of Escherichia coli K-12 through a multi-hit kinetics interaction. AS-48 causes a parallel and gradual cessation of all biosynthetic pathways monitored (protein, RNA, DNA, and cell wall synthesis), the rate of incorporation of labeled precursors, the rate of O2 consumption, and cell growth. These effects have been attributed to alterations of cytoplasmic membrane functions.Key words: Escherichia coli, peptide antibiotic, bactericide.


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