Isolation, characterization and physiological properties of an autolytic-deficient mutant of Streptococcus pneumoniae
- 1 August 1986
- journal article
- research article
- Published by Springer Nature in Molecular Genetics and Genomics
- Vol. 204 (2), 237-242
- https://doi.org/10.1007/bf00425504
Abstract
Summary A spontaneous mutation in the gene lyt encoding the pneumococcal autolysin has been characterized. This mutation, named lyt-32, which behaves as a high-efficiency marker in pneumococcal transformation, is a single base pair GC deletion causing the appearance of two consecutive termination codons in the amino terminal part of the sequence of the autolysin gene. The mutant lyt gene did not code for a polypeptide of relative molecular mass corresponding to the pneumococcal E form amidase in Escherichia coli maxicells. Pneumococcal cells containing the lyt-32 mutation (M32) were fully transformable, multiplied at a normal growth rate forming small chains and showed a tolerant response when treated with beta-lactam antibiotics. Strain M32 represents the first example of a mutant of Streptococcus pneumoniae completely lacking amidase as a consequence of an alteration in the structural gene coding for the pneumococcal autolysin.Keywords
This publication has 28 references indexed in Scilit:
- Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coliGene, 1986
- Cloning and expression of the pneumococcal autolysin gene in Escherichia coliMolecular Genetics and Genomics, 1985
- A rapid procedure to detect the autolysin phenotype in Streptococcus pneumoniaeFEMS Microbiology Letters, 1985
- Interaction of the pneumococcal amidase with lipoteichoic acid and cholineEuropean Journal of Biochemistry, 1985
- Restriction cleavage maps of the DNAs of Streptococcus pneumoniae bacteriophages containing protein covalently bound to their 5′ endsMolecular Genetics and Genomics, 1984
- Inhibition of lysis by antibody against phage-associated lysin and requirement of choline residues in the cell wall for progeny phage release inStreptococcus pneumoniaeCurrent Microbiology, 1983
- A system for shotgun DNA sequencingNucleic Acids Research, 1981
- On the physiological functions of teichoic acidsJournal of Supramolecular Structure, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- A complementation analysis of the restriction and modification of DNA in Escherichia coliJournal of Molecular Biology, 1969