PMID:10869073

Citation	Fournier, B and Hooper, DC (2000) A new two-component regulatory system involved in adhesion, autolysis, and extracellular proteolytic activity of Staphylococcus aureus. J. Bacteriol. 182:3955-64
Abstract	A transposition mutant of Staphylococcus aureus was selected from the parent strain MT23142, a derivative of strain 8325. The site of transposition was near the 5' terminus of the gene arlS. ArlS exhibits strong similarities with histidine protein kinases. Sequence analysis suggested that arlS forms an operon with upstream gene arlR. The predicted product of arlR is a member of the OmpR-PhoB family of response regulators. The arlS mutant formed a biofilm on a polystyrene surface unlike the parent strain and the complemented mutant. Biofilm formation was associated with increased primary adherence to polystyrene, whereas cellular adhesion was only slightly decreased. In addition, the arlS mutant exhibited increased autolysis and altered peptidoglycan hydrolase activity compared to the parental strain and to the complemented mutant. As it has been shown for coagulase-negative staphylococci that some autolysins are able to bind polymer surfaces, these data suggest that the two-component regulatory system ArlS-ArlR may control attachment to polymer surfaces by affecting secreted peptidoglycan hydrolase activity. Finally, the arlS mutant showed a dramatic decrease of extracellular proteolytic activity, including serine protease activity, in comparison to the wild-type strain and the complemented mutant, and cells grown in the presence of phenylmethylsulfonyl fluoride (a serine protease inhibitor) showed an increased autolysin activity. Since the locus arlR-arlS strikingly modifies extracellular proteolytic activity, this locus might also be involved in the virulence of S. aureus.
Links	PubMed PMC94580
Keywords	Amino Acid Sequence; Anti-Bacterial Agents/pharmacology; Bacterial Adhesion/genetics; Bacterial Proteins/genetics; Bacteriolysis/genetics; Cell Wall/drug effects; Endopeptidases/metabolism; Genetic Complementation Test; Metals, Heavy/pharmacology; Molecular Sequence Data; Mutagenesis, Insertional; Potassium Chloride/pharmacology; Protein Kinases/genetics; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Signal Transduction/genetics; Sodium Chloride/pharmacology; Staphylococcus aureus/cytology; Staphylococcus aureus/genetics; Staphylococcus aureus/pathogenicity
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
STAA3:ARLS		GO:0000155: phosphorelay sensor kinase activity	ECO:0000315:		F		Table 2. The mutant showed less extracellular proteolytic activity. Which in turn is responsible for increased autolysis of mutant cells. Could very well be part of the reason S. aureus is virulent.	complete CACAO 9594
STAA8:ARLS		GO:0043709: cell adhesion involved in single-species biofilm formation	ECO:0000315:		P		Fig. 2: arlS mutant (BF16) formed a film on surface of microtiter plates, no such film was seen in plates with wild-type and complemented strains	complete CACAO 9666
STAA8:ARLS		GO:0009405: pathogenesis	ECO:0000315:		P		Table 2: The mutant showed less extracellular proteolytic activity, which is responsible for increased autolysis of mutant cells.	complete CACAO 9840
STAA8:ARLS		GO:0000155: phosphorelay sensor kinase activity	ECO:0000315:		F		Table 2. The mutant showed less extracellular proteolytic activity. Which is responsible for increased autolysis of mutant cell	complete CACAO 10025
STAA8:ARLS		GO:0008236: serine-type peptidase activity	ECO:0000315:		F		Table 2 Arls mutant strains showed a decrease in serine protease activity and an increase in autolysin activity when exposed to a serine protease inhibitor	complete CACAO 10031
STAA8:ARLS	enables	GO:0008236: serine-type peptidase activity	ECO:0000315: mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete

References

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