scholarly journals Characterization of the Bacillus subtilis Penicillin-Binding Protein PBP4

2019 ◽  
Vol 09 (03) ◽  
pp. 164-176
Author(s):  
Arnaud Vanden Broeck ◽  
Eric Sauvage ◽  
Bernard Joris ◽  
Colette Duez
Keyword(s):  
Bacillus Subtilis ◽  
Binding Protein ◽  
Penicillin Binding Protein

scholarly journals Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis

1998 ◽  
Vol 180 (18) ◽  
pp. 4967-4973 ◽  
Author(s):  
Lotte B. Pedersen ◽  
Thomas Murray ◽  
David L. Popham ◽  
Peter Setlow
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Binding Protein ◽  
Low Molecular Weight ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Genome Sequencing Project ◽  
Penicillin Binding Proteins ◽  
Sequencing Project

ABSTRACT The pbp gene (renamed dacC), identified by the Bacillus subtilis genome sequencing project, encodes a putative 491-residue protein with sequence homology to low-molecular-weight penicillin-binding proteins. Use of a transcriptional dacC-lacZ fusion revealed thatdacC expression (i) is initiated at the end of stationary phase; (ii) depends strongly on transcription factor ςH; and (iii) appears to be initiated from a promoter located immediately upstream of yoxA, a gene of unknown function located upstream of dacC on the B. subtilis chromosome. A B. subtilis dacCinsertional mutant grew and sporulated identically to wild-type cells, and dacC and wild-type spores had the same heat resistance, cortex structure, and germination and outgrowth kinetics. Expression ofdacC in Escherichia coli showed that this gene encodes an ∼59-kDa membrane-associated penicillin-binding protein which is highly toxic when overexpressed.

Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis

Gene ◽  
2000 ◽  
Vol 246 (1-2) ◽  
pp. 187-196 ◽  
Author(s):  
L.B. Pedersen ◽  
K. Ragkousi ◽  
T.J. Cammett ◽  
E. Melly ◽  
A. Sekowska ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Binding Protein ◽  
Weight Class ◽  
Penicillin Binding Protein ◽  
Class A

scholarly journals Identification and Characterization of the Penicillin-Binding Protein 2a of Streptococcus pneumoniae and Its Possible Role in Resistance to β-Lactam Antibiotics

2000 ◽  
Vol 44 (6) ◽  
pp. 1745-1748 ◽  
Author(s):  
Genshi Zhao ◽  
Timothy I. Meier ◽  
Joann Hoskins ◽  
Kelly A. McAllister
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Protein ◽  
Penicillin Resistance ◽  
Penicillin Binding Protein ◽  
Insertional Mutant ◽  
Identification And Characterization

ABSTRACT To further understand the role of penicillin-binding protein 2a (PBP 2a) of Streptococcus pneumoniae in penicillin resistance, we confirmed the identity of the protein as PBP 2a. The PBP 2a protein migrated electrophoretically to a position corresponding to that of PBP 2x, PBP 2a, and PBP 2b of S. pneumoniae and was absent in a pbp2ainsertional mutant of S. pneumoniae. We found that the affinities of PBP 2a for penicillins were lower than for cephalosporins and a carbapenem. When compared with other S. pneumoniae PBPs, PBP 2a exhibited lower affinities for β-lactam antibiotics, especially penicillins. Therefore, PBP 2a is a low-affinity PBP for β-lactam antibiotics in S. pneumoniae.

Sign in / Sign up

Export Citation Format

Share Document