Identification and characterization of an autolysin gene, atlg, from Streptococcus sobrinus.
AtlA is a major cell-lytic enzyme called autolysin in Streptococcus mutans. In this study, we identified the atlg gene-encoding autolysin (Atlg), consisting of 863 residues from Streptococcus sobrinus 6715DP, and confirmed lytic activity of recombinant Atlg by zymography of S. sobrinus cells. An atlA-inactivated mutant was constructed in S. mutans Xc, and the atlg gene product was characterized by plasmid complementation. Microscopic analysis, saliva-induced aggregation assay and autolysis assay of static cultures in air revealed that the atlg gene product partially complemented the role of AtlA. Furthermore, the capability of biofilm formation of the atlA-deficient mutant cultivated in air was restored by plasmid comprising the atlg gene. These findings suggest that Atlg may be involved in cell separation and biofilm formation in S. sobrinus.
Yamada
Arisa
A
Department of Dental Pharmacology, School of Dentistry, Iwate Medical University, Morioka, Japan.
Tamura
Haruki
H
Kato
Hirohisa
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018441:Biofilms; D006801:Humans; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012463:Saliva / Q000382:microbiology; D016415:Sequence Alignment; D013295:Streptococcus mutans / Q000235:genetics / Q000378:metabolism; D016986:Streptococcus sobrinus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000502:physiology
D001426:Bacterial Proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase