Article Abstract:
Chorismate synthase is an enzyme of the aromatic biosynthetic pathway that has been widely studied in a number of microorganisms but not in Staphylococcus aureus. Molecular analyses of chorismate synthase in S. aureus identified aroC, which encodes the enzyme, and ndk, which encodes nucleoside diphosphate kinase. Located upstream of ndk was gerCC while gerCA and gerCB genes were found downstream of ndk. The enyzme exhibited a homotetramer structure with a molecular mass of 43024 daltons.
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Article Abstract:
Results describe ten new LPXTG proteins from Staphylococcus aureus genome sequences out of a total of 21 that the bacterium can express. Data show that in eight of the ten the cell-wall sorting signal LPXTG covalently anchors the proteins to the cell-wall peptidoglycan, while the remaining two differ in a single residue at the fourth position of the LPXTG motif. The LPXTG-anchored surface proteins may have originated in a modular fashion.
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Article Abstract:
The mapping of the cap5(8) locus on the Staphylococcus aureaus chromosome and the nucleotide sequences of the cap5 and cap8 gene clusters were reported. It was found that the DNA sequences which contain 12 of the 16 open reading frames of the cap5 and cap8 gene clusters are almost identical. The possible functions of these open reading in CP5 and CP8 biosynthesis were also discussed.
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