scholarly journals The PASTA domain of penicillin-binding protein SpoVD is dispensable for endospore cortex peptidoglycan assembly in Bacillus subtilis

Microbiology ◽  
2015 ◽  
Vol 161 (2) ◽  
pp. 330-340 ◽  
Author(s):  
Ewa Bukowska-Faniband ◽  
Lars Hederstedt
Keyword(s):  
Bacillus Subtilis ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Pasta Domain

scholarly journals The sporulation-specific penicillin-binding protein 5a from Bacillus subtilis is a dd-carboxypeptidase in vitro

1985 ◽  
Vol 230 (3) ◽  
pp. 825-828 ◽  
Author(s):  
John A. Todd ◽  
Eileen J. Bone ◽  
David J. Ellar
Keyword(s):  
Bacillus Subtilis ◽  
Binding Protein ◽  
Penicillin Binding Protein

The sporulation-specific penicillin-binding protein 5a was purified from Bacillus subtilis and shown to possess dd-carboxypeptidase activity in vitro.

scholarly journals Analysis of Outgrowth of Bacillus subtilis Spores Lacking Penicillin-Binding Protein 2a

1998 ◽  
Vol 180 (24) ◽  
pp. 6493-6502 ◽  
Author(s):  
Thomas Murray ◽  
David L. Popham ◽  
Christine B. Pearson ◽  
Arthur R. Hand ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Cell Elongation ◽  
Binding Protein ◽  
Divalent Cations ◽  
Cross Linking ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Spore Outgrowth ◽  
Partial Redundancy

ABSTRACT The loss of Bacillus subtilis penicillin-binding protein (PBP) 2a, encoded by pbpA, was previously shown to slow spore outgrowth and result in an increased diameter of the outgrowing spore. Further analyses to define the defect inpbpA spore outgrowth have shown that (i) outgrowingpbpA spores exhibited only a slight defect in the rate of peptidoglycan (PG) synthesis compared to wild-type spores, but PG turnover was significantly slowed during outgrowth of pbpAspores; (ii) there was no difference in the location of PG synthesis in outgrowing wild-type and pbpA spores once cell elongation had been initiated; (iii) outgrowth and elongation of pbpAspores were dramatically affected by the levels of monovalent or divalent cations in the medium; (iv) there was a partial redundancy of function between PBP2a and PBP1 or -4 during spore outgrowth; and (v) there was no difference in the structure of PG from outgrowing wild-type spores or spores lacking PBP2a or PBP2a and -4; but also (vi) PG from outgrowing spores lacking PBP1 and -2a had transiently decreased cross-linking compared to PG from outgrowing wild-type spores, possibly due to the loss of transpeptidase activity.

scholarly journals Transcriptional Analysis of theStaphylococcus aureus Penicillin Binding Protein 2 Gene

1998 ◽  
Vol 180 (23) ◽  
pp. 6077-6081 ◽  
Author(s):  
Mariana G. Pinho ◽  
Herminia de Lencastre ◽  
Alexander Tomasz
Keyword(s):  
Bacillus Subtilis ◽  
Methicillin Resistance ◽  
Binding Protein ◽  
Primer Extension ◽  
Full Recovery ◽  
Transcriptional Analysis ◽  
High Homology ◽  
Penicillin Binding Protein ◽  
High Level

ABSTRACT Sequencing of the vicinity of the staphylococcal pbp2gene and transcriptional analysis by primer extension and promoter fusions were used to show that pbp2 is part of an operon that also includes a gene with high homology to prfA ofBacillus subtilis. Two distinct promoters were identified directing transcription of pbp2 either alone or together with prfA. It was recently reported that transposon inactivation of pbp2 causes a reduction in methicillin resistance, but complementation experiments were not fully successful. We now show that introduction of the intact pbp2 gene with its two newly identified promoters into the chromosome of the transposon mutant resulted in the full recovery of high-level methicillin resistance.

scholarly journals A Mother Cell-Specific Class B Penicillin-Binding Protein, PBP4b, in Bacillus subtilis

2004 ◽  
Vol 186 (1) ◽  
pp. 258-261 ◽  
Author(s):  
Yuping Wei ◽  
Derrell C. McPherson ◽  
David L. Popham
Keyword(s):  
Bacillus Subtilis ◽  
Rna Polymerase ◽  
Mother Cell ◽  
Binding Proteins ◽  
Binding Protein ◽  
Specific Class ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins ◽  
Peptidoglycan Structure ◽  
Class B

ABSTRACT The Bacillus subtilis genome encodes 16 penicillin-binding proteins (PBPs), some of which are involved in synthesis of the spore peptidoglycan. The pbpI (yrrR) gene encodes a class B PBP, PBP4b, and is transcribed in the mother cell by RNA polymerase containing σE. Loss of PBP4b, alone and in combination with other sporulation-specific PBPs, had no effect on spore peptidoglycan structure.

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
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