The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis

1994 ◽  
Vol 12 (4) ◽  
pp. 535-545 ◽  
Author(s):  
Philippe Margot ◽  
Catherine Mauël ◽  
Dimitri Karamata
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Vegetative Cell ◽  
Bacillus Subtilis 168 ◽  
Cell Wall Hydrolase ◽  
Cell Autolysis

scholarly journals The lytE Gene of Bacillus subtilis 168 Encodes a Cell Wall Hydrolase

1998 ◽  
Vol 180 (8) ◽  
pp. 2272-2272
Author(s):  
Philippe Margot ◽  
Michael Whalen ◽  
Ahmad Gholamhoseinian ◽  
Patrick Piggot ◽  
Dimitri Karamata
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Bacillus Subtilis 168 ◽  
Cell Wall Hydrolase ◽  
A Cell

scholarly journals The lytE Gene of Bacillus subtilis 168 Encodes a Cell Wall Hydrolase

1998 ◽  
Vol 180 (3) ◽  
pp. 749-752 ◽  
Author(s):  
Philippe Margot ◽  
Michael Wahlen ◽  
Ahmad Gholamhuseinian ◽  
Patrick Piggot ◽  
Dimitri Karamata
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Walls ◽  
Exponential Growth Phase ◽  
Terminal Domain ◽  
Bacillus Subtilis 168 ◽  
Phase Sequence ◽  
Cell Autolysis ◽  
A Cell ◽  
Repeated Motif

ABSTRACT Bacillus subtilis cell wall-bound protein CWBP33 is encoded by lytE, a gene expressed during the exponential growth phase. Sequence analysis of LytE, a 33-kDa protein, reveals two domains. The N-terminal domain contains a threefold-repeated motif common to several peptidoglycan binding proteins, while the C-terminal domain, probably carrying the catalytic activity, has homology with certain exoproteins. Zymographs unambiguously reveal that the absence of CWBP33, due to inactivation of lytE, is accompanied by the loss of a lytic activity. In lytE mutants, the cell autolysis rate is significantly decreased, although autolysis of corresponding, purified cell walls does not seem to be affected.

scholarly journals Nucleotide sequence and regulation of a new putative cell wall hydrolase gene, cwlD, which affects germination in Bacillus subtilis. .

1995 ◽  
Vol 177 (19) ◽  
pp. 5582-5589 ◽  
Author(s):  
J Sekiguchi ◽  
K Akeo ◽  
H Yamamoto ◽  
F K Khasanov ◽  
J C Alonso ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Nucleotide Sequence ◽  
Cell Wall Hydrolase

scholarly journals SweC and SweD are essential co-factors of the FtsEX-CwlO cell wall hydrolase complex in Bacillus subtilis

PLoS Genetics ◽  
2019 ◽  
Vol 15 (8) ◽  
pp. e1008296 ◽  
Author(s):  
Yannick R. Brunet ◽  
Xindan Wang ◽  
David Z. Rudner
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Wall Hydrolase

scholarly journals Analysis of Peptidoglycan Structure from Vegetative Cells of Bacillus subtilis 168 and Role of PBP 5 in Peptidoglycan Maturation

1999 ◽  
Vol 181 (13) ◽  
pp. 3956-3966 ◽  
Author(s):  
Abdelmadjid Atrih ◽  
Gerold Bacher ◽  
Günter Allmaier ◽  
Michael P. Williamson ◽  
Simon J. Foster
Keyword(s):  
Bacillus Subtilis ◽  
Vegetative Cell ◽  
Gel Filtration ◽  
Diaminopimelic Acid ◽  
Growth Media ◽  
Side Chains ◽  
Anionic Polymers ◽  
Bacillus Subtilis 168 ◽  
A Value ◽  
Attachment Sites

ABSTRACT The composition and fine structure of the vegetative cell wall peptidoglycan from Bacillus subtilis were determined by analysis of its constituent muropeptides. The structures of 39 muropeptides, representing 97% of the total peptidoglycan, were elucidated. About 99% analyzed muropeptides in B. subtilisvegetative cell peptidoglycan have the free carboxylic group of diaminopimelic acid amidated. Anhydromuropeptides and products missing a glucosamine at the nonreducing terminus account for 0.4 and 1.5%, respectively, of the total muropeptides. These two types of muropeptides are suggested to end glycan strands. An unexpected feature of B. subtilis muropeptides was the occurrence of a glycine residue in position 5 of the peptide side chain on monomers or oligomers, which account for 2.7% of the total muropeptides. This amount is, however, dependent on the composition of the growth media. Potential attachment sites for anionic polymers to peptidoglycan occur on dominant muropeptides and account for 2.1% of the total. B. subtilis peptidoglycan is incompletely digested by lysozyme due to de-N-acetylation of glucosamine, which occurs on 17.3% of muropeptides. The cross-linking index of the polymer changes with the growth phase. It is highest in late stationary phase, with a value of 33.2 or 44% per muramic acid residue, as determined by reverse-phase high-pressure liquid chromatography or gel filtration, respectively. Analysis of the muropeptide composition of a dacA (PBP 5) mutant shows a dramatic decrease of muropeptides with tripeptide side chains and an increase or appearance of muropeptides with pentapeptide side chains in monomers or oligomers. The total muropeptides with pentapeptide side chains accounts for almost 82% in thedacA mutant. This major low-molecular-weight PBP (dd-carboxypeptidase) is suggested to play a role in peptidoglycan maturation.

scholarly journals Regulation of a New Cell Wall Hydrolase Gene,cwlF, Which Affects Cell Separation in Bacillus subtilis

1998 ◽  
Vol 180 (9) ◽  
pp. 2549-2555 ◽  
Author(s):  
Shu Ishikawa ◽  
Yoshiko Hara ◽  
Ryo Ohnishi ◽  
Junichi Sekiguchi
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Rna Polymerase ◽  
Sequence Similarity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exponential Growth Phase ◽  
High Sequence Similarity ◽  
Cell Wall Hydrolase ◽  
Mutant Cells

ABSTRACT Bacillus subtilis produces a 35-kDa cell wall hydrolase, CwlF, during vegetative growth. The CwlF protein was extracted from B. subtilis cwlB sigD mutant cells and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. N-terminal amino acid sequencing revealed that its sequence is completely identical to that of the internal region of thepapQ gene product. Disruption of the papQ gene in the B. subtilis chromosome led to the complete loss of CwlF, indicating that papQ is identical tocwlF. CwlF exhibits high sequence similarity to the p60 proteins of Listeria species, NlpC proteins ofEscherichia coli and Haemophilus influenzae, and Enp2 protein of Bacillus sphaericus. The β-galactosidase activity of the cwlF-lacZ transcriptional fusion and Northern blot analysis of the cwlF gene indicated that the gene is expressed as a monocistronic operon during the exponential growth phase, and primer extension analysis suggested that the cwlF gene is transcribed mainly by EςA RNA polymerase and weakly by EςH RNA polymerase. While the cells of the cwlF-deficient mutant were about twice as long as those of the wild-type strain, the cwlF sigD double mutant cells exhibited extraordinary microfiber formation, in contrast to the filamentation of the sigD mutant. The CwlF production was not affected by the pleiotropic mutationsflaD1 and degU32(Hy), which endow cells with the ability of extensive filamentation.

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