Staphylococcus aureus sequence

Figure 10.1 shows a two-dimensional [15N, H]-TROSY correlation spectrum of the 15N,2H- labeled 110 kDa homo-octameric protein 7,8-dihydroneopterin aldolase from Staphylococcus aureus (DHNA) measured with the pulse sequence of Fig. 10.4 [13]. The gain in spectral resolution and sensitivity is readily apparent from comparison with the corresponding conventional experiment. The optimal sensitivity is achieved by adjusting the polarization transfer r in Fig. 10.4 (3 ms <2r<5.4 ms [3]). For an optimal suppression of the non-TROSY components, the so-called Clean TROSY might be used [19]. Similar signal and spectral resolution enhancements are achieved for 15N,2H-labeled or 13C,15N,2H-...

In contrast to Gram-negatives, many Gram-positive bacteria employ post-translationally modified peptides processed from larger precursors as QS signal molecules. In Staphylococcus aureus, for example, a family of peptide (7-9 amino acid residues) thiolactones which vary in the primary amino acid sequence but contain a conserved cysteine at position 5 control the expression of cell wall colonization factors and exotoxins [24-26]. 

Laddaga, R. A., Chu, L., Mistra, T. K. Silver, S. 1987. Nucleotide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258. Proceedings of the National Academy of Science USA, 84, 5106-10. 

Fig. 2. Amino acid sequences of /3-lactamases of Staphylococcus aureus PCI (upper line) and of BadUus lickeniformis 749/C ments LA to LE, lower line). Matching residues are shown in block letters (upper line). (From Ambler and Meadway, 63.)... 

Nuclease is composed of 149 amino acid residues, and contains neither sulfhydryl groups nor disulfide bonds (20, 25, 26). Figure 1 shows the amino acid sequence of nuclease isolated from Staphylococcus aureus, strain V8 (20, 25-27). Physical measurements of the molecular weight of nuclease from strain V8 as well as from strain Foggi are consistent with this sequence (28). 

When calcineurin B was digested with Staphylococcus aureus proteinase, a peptide, SP1, lacking a free NH -terminal amino acid was also eluted from HPLC at 57% acetonitrile. Amino acid analysis showed it to be a tripeptide Gly,Asx,Glx. From the known specificity of S. aureus proteinase the C-terminal reside of SP1 must be Glu. FAB mass spectrometry established the of SP1 as 528, and esterification of this peptide led to an increase in to 556, which corresponds to the formation of two methyl esters. Since SP1 has two free carboxyl groups, the sequence of SP1 must be X-(Gly,Asn)-Glu and the of the blocking group must be 211. 

Kuroda, M. et al. 2001. Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357, 1225-1240. 

For example, in cultures of Bacillus subtilis, protein synthesis had ceased entirely after one fourth of a doubling time when RNA synthesis was specifically and completely inhibited by actionomycin D33. Since the initiation of a new round of DNA biosynthesis requires the ad hoc synthesis of initiator protein(s), DNA biosynthesis comes to a standstill after a lag as the result of the failure of initiator protein synthesis. This interesting sequence of events was first described by Kirk34 for the action of actinomycin D in Staphylococcus aureus. 

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