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- W1505519692 abstract "A major Bacillus subtilis 168S autolysin (N-acetylmuramoyl-L-alanine amidase [EC 3.5.1.28]) was purified and then cleaved with cyanogen bromide. The N-terminal amino acid sequence of one of the resultant peptides was determined in order to make synthetic oligonucleotides. A 2.5-kb EcoRI fragment was cloned into Escherichia coli JM109 and detected by colony hybridization by using the oligonucleotides as probes. Sequencing of the insert showed the presence of an open reading frame (designated cwlB), starting at a UUG codon, which encodes a polypeptide of 496 amino acids with a molecular mass of 52,623 Da. CWLB had a presumed signal peptide which is processed after Ala at position 24. Insertional inactivation of the cwlB gene of the B. subtilis chromosome led to an approximately 90% decrease in the total cell wall hydrolytic activity of stationary-phase cells and extraordinary resistance to cell lysis, even after 6 days of incubation at 37 degrees C. No apparent changes in cell morphology, motility, competence, sporulation, or germination were observed." @default.
- W1505519692 created "2016-06-24" @default.
- W1505519692 creator A5025139576 @default.
- W1505519692 creator A5048290923 @default.
- W1505519692 date "1991-11-01" @default.
- W1505519692 modified "2023-10-16" @default.
- W1505519692 title "Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene" @default.
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- W1505519692 doi "https://doi.org/10.1128/jb.173.22.7304-7312.1991" @default.
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