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 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.

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 Septal Localization of Penicillin-Binding Protein 1 in Bacillus subtilis

1999 ◽  
Vol 181 (10) ◽  
pp. 3201-3211 ◽  
Author(s):  
Lotte B. Pedersen ◽  
Esther R. Angert ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Immunofluorescence Microscopy ◽  
Binding Protein ◽  
Divalent Cations ◽  
Significant Proportion ◽  
Growth Media ◽  
Weight Class ◽  
Penicillin Binding Protein ◽  
Septal Localization ◽  
Mutant Cells

ABSTRACT Previous studies have shown that Bacillus subtiliscells lacking penicillin-binding protein 1 (PBP1), encoded byponA, have a reduced growth rate in a variety of growth media and are longer, thinner, and more bent than wild-type cells. It was also recently shown that cells lacking PBP1 require increased levels of divalent cations for growth and are either unable to grow or grow as filaments in media low in Mg2+, suggesting a possible involvement of PBP1 in septum formation under these conditions. Using epitope-tagging and immunofluorescence microscopy, we have now shown that PBP1 is localized at division sites in vegetative cells of B. subtilis. In addition, we have used fluorescence and electron microscopy to show that growingponA mutant cells display a significant septation defect, and finally by immunofluorescence microscopy we have found that while FtsZ localizes normally in most ponA mutant cells, a significant proportion of ponA mutant cells display FtsZ rings with aberrant structure or improper localization, suggesting that lack of PBP1 affects FtsZ ring stability or assembly. These results provide strong evidence that PBP1 is localized to and has an important function in the division septum in B. subtilis. This is the first example of a high-molecular-weight class A PBP that is localized to the bacterial division septum.

scholarly journals Purification and Characterization of PBP4a, a New Low-Molecular-Weight Penicillin-Binding Protein fromBacillus subtilis

2001 ◽  
Vol 183 (5) ◽  
pp. 1595-1599 ◽  
Author(s):  
Colette Duez ◽  
Marc Vanhove ◽  
Xavier Gallet ◽  
Fabrice Bouillenne ◽  
Jean-Denis Docquier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Binding Protein ◽  
Order Rate Constant ◽  
Low Molecular Weight ◽  
Penicillin Binding Protein ◽  
Purification And Characterization ◽  
The Third

ABSTRACT Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits dd-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frère, and J. M. Ghuysen, Biochem. J. 282:781–788, 1992), which is rapidly inactivated by many β-lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k 2/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M−1s−1 for the Actinomadura sp. strain R39 peptidase, 1,400 M−1 s−1 for B. subtilis PBP4a, and 7,000 M−1 s−1 forEscherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k 2/K = 46,000 M−1 s−1). PBP4a is also much more thermostable than the R39 enzyme.

Sign in / Sign up

Export Citation Format

Share Document