1887

Abstract

The class I fructose 1,6-diphosphate aldolases of five staphylococcal strains were purified and characterized. All of these enzymes could be renatured to active structures after exposure to a temperature of 90°C. By using antisera against the enzymes, we measured the immunological cross-reactions by microcomplement fixation and activity inhibition. The amino acid compositions of the purified proteins were determined and compared. Our results provide further insight into the phylogenetical relationships among the staphylococcal species studied. , and form a group of highly related species. was shown to be closely related to this group, whereas all of the other staphylococcal species showed distant relationships. subsp. and subsp. occupy a rather isolated position within the genus and are related to each other at the species level.

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1983-07-01
2024-12-10
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References

  1. Baldwin S. A., Perham R. N., Stribling D. 1978; Purification and characterization of the class II d-fructose-1,6-biphosphate aldolase from E. coli (Crookes strain). Biochem. J. 169:633–641
    [Google Scholar]
  2. Champion A. B., Prager E. M., Wachter D., Wilson A. C. 1974; Microcomplement fixation. 397–416 Wright C. A. Biochemical and immunological taxonomy of animals—1974 Academic Press, Inc.; London:
    [Google Scholar]
  3. Champion A. B., Soderberg K. L., Wilson A. C., Ambler P. P. 1975; Immunological comparison of azurins of known amino acid sequence. J. Mol. Evol. 5:291–305
    [Google Scholar]
  4. Cornish-Bowden A. 1981; Interpretation of amino acid compositions. Trends Biochem. Sci. 6:217–219
    [Google Scholar]
  5. Crumpton M. J. 1974; Protein antigens: the molecular bases of antigenicity and immunogenicity. 1–78 Sela M. The antigens 2 Academic Press, Inc.; New York:
    [Google Scholar]
  6. Fischer S., Luczak H., Schleifer K. H. 1982; Improved methods for the detection of class I and class II fructose-1,6-bisphosphate aldolases in bacteria. FEMS Microbiol. Lett. 15:103–108
    [Google Scholar]
  7. Goodfellow M., Mordarski M., Tkacz A., Szyba K., Pulverer G. 1980; Polynucleotide sequence divergence among some coagulase negative staphylococci. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. 1 Orig. Reihe A 246:10–22
    [Google Scholar]
  8. Gotz F., Fischer S., Schleifer K. H. 1980; Purification and characterization of an unusually heat-stable and acidfàase stable class I fructose-1,6-bisphosphate aldolase from S. aureus . Eur. J. Biochem. 108:295–301
    [Google Scholar]
  9. Götz F., Nürnberger E., Schleifer K. H. 1979; Distribution of class I and class II d-fructose-1,6-bisphosphate aldolases in various staphylococci, peptococci and micrococci. FEMS Microbiol. Lett. 5:253–257
    [Google Scholar]
  10. Harris C. E., Kobes R. D., Teller D. C., Rutter W. J. 1969; The molecular characteristics of yeast aldolase. Biochemistry 8:2442–2454
    [Google Scholar]
  11. Harris C. E., Teller D. C. 1973; Estimation of primary sequence homology from amino acid composition of evolutionary related proteins. J. Theor. Biol. 38:347–362
    [Google Scholar]
  12. Horecker B. L., Tsolas O., Lai C. Y. 1972; Aldolases. 213–258 Boyer P. D. The enzymes, 3. 7 Academic Press, Inc.; New York:
    [Google Scholar]
  13. Jayanthi Bai N., Ramachandra Pai M., Suryanarayana Murthy P., Venkitasubramanian T. A. 1975; Fructose diphosphate aldolase from Mycobacterium smegmatis. Purification and properties. Arch. Biochem. Biophys. 168:230–234
    [Google Scholar]
  14. Kilpper R., Buhl K., Schleifer K. H. 1980; Nucleic acid homology studies between P. saccharolyticus and various anaerobic and facultative anaerobic Gram-positive cocci. FEMS Microbiol. Lett. 8:205–210
    [Google Scholar]
  15. Kilpper-Bälz R., Schleifer K. H. 1981; Transfer of Peptococcus saccharolyticus Foubert and Douglas to the genus Staphylococcus: Staphylococcus saccharolyticus (Foubert and Douglas) comb. nov. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. 1 Orig. Reihe C 2:331–334
    [Google Scholar]
  16. Kloos W. E. 1980; Natural populations of the genus Staphylococcus . Annu. Rev. Microbiol. 34:559–592
    [Google Scholar]
  17. Kloos W. E., Wolfshohl J. F. 1979; Evidence for deoxyribonucleotide sequence divergence between staph-ylococci living on human and other primate skin. Curr. Microbiol. 3:167–172
    [Google Scholar]
  18. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685
    [Google Scholar]
  19. Lebherz H. G., Bradshaw R. A., Rutter W. J. 1973; Structural comparisons between the class I fructose diphosphate aldolases from Micrococcus aerogenes and rabbit. J. Biol. Chem. 248:1660–1665
    [Google Scholar]
  20. Lebherz H. G., Rutter W. J. 1973; A class I (Schiffbase) fructose diphosphate aldolase of procaryotic origin. J. Biol. Chem. 248:1650–1659
    [Google Scholar]
  21. London J. 1974; Variations in the quarternary structure of three lactic acid bacteria aldolases. J. Biol. Chem. 249:7977–7983
    [Google Scholar]
  22. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275
    [Google Scholar]
  23. Ludwig W., Schleifer K. H., Fox G. E., Seewaldt E., Stackebrandt E. 1981; Phylogenetic analysis of staphylococci, Peptococcus saccharolyticus and Micrococcus mucilaginosus . J. Gen. Microbiol. 125:357–366
    [Google Scholar]
  24. Meyer S. A., Schleifer K. H. 1978; Deoxyribonucleic acid reassociation in the classification of coagulase-positive staphylococci. Arch. Microbiol. 117:183–188
    [Google Scholar]
  25. Moore S., Stein H. 1963; Chromatographic determination of amino acids by the use of automatic recording equipment. Methods Enzymol. 16:819–831
    [Google Scholar]
  26. Pajot P. 1976; Fluorescence of proteins in 6 M guanidine hydrochloride. Eur. J. Biochem. 63:263–269
    [Google Scholar]
  27. Penhoe E., Kochmann M., Rutter W. J. 1969; Molecular and catalytic properties of aldolase C. Biochemistry 8:4396–4402
    [Google Scholar]
  28. Prager E. M., Wilson A. C. 1971; The dependence of immunological cross reactivity upon sequence resemblance among lysozymes. I. Microcomplement fixation studies. J. Biol. Chem. 246:5978–5980
    [Google Scholar]
  29. Rosenbluhm E. D., Tyrone S. 1979; Deoxyribonucleic acid homologies among staphylococci: coagulase positive reference strains. Curr. Microbiol. 2:171–174
    [Google Scholar]
  30. Rupprecht M., Schleifer K. H. 1979; A comparative immunological study of catalases from coagulase positive staphylococci. Arch. Microbiol. 120:53–56
    [Google Scholar]
  31. Rutter W. J. 1964; Evolution of aldolase. Fed. Proc. 23:1248–1257
    [Google Scholar]
  32. Schleifer K. H., Meyer S. A., Rupprecht M. 1979; Relatedness among coagulase-negative staphylococci: deoxyribonucleic acid reassociation and comparative immunological studies. Arch. Microbiol. 122:93–101
    [Google Scholar]
  33. Schram E., Moore S., Bigwood E. J. 1954; Chromatographic determination of cysteine as cysteic acid. Biochem. J. 57:33–41
    [Google Scholar]
  34. Stackebrandt E., Lewis B. J., Woese C. R. 1980; The phylogenetic structures of the coryneform group of bacteria. Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. 1 Orig. Reihe C 1:137–149
    [Google Scholar]
  35. Stribling D., Perham R. N. 1973; Purification and characterization of two fructose diphosphate aldolases from E. coli (Crookes strain). Biochem. J. 131:833–841
    [Google Scholar]
  36. Tsugita A., Scheffler J. J. 1982; A new rapid method for acid hydrolysis of protein. Proc. Jpn. Acad. 58: (Ser. B) 1–4
    [Google Scholar]
  37. Weber K., Osborn M. 1969; The reliability of molecular weight determination by dodecyl sulphate poly-acrylamide gel electrophoresis. J. Biol. Chem. 244:4406–4412
    [Google Scholar]
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