Archives of Microbiology

, Volume 147, Issue 2, pp 158–162 | Cite as

Environmental control of protein export of Bacillus licheniformis NCIB 6346 reveals two types of extracellular proteins

  • M. J. Lancaster
  • C. W. Keevil
  • D. C. Ellwood
  • R. C. W. Berkeley
Original Papers
Received:
Accepted:

Abstract

Teichuronic acid was the major anionic polymer of Bacillus licheniformis NCIB 6346 durign phosphate-limited (P-limited) growth in the chemostat. This polymer was also present in significant quantities when B. licheniformis was grown under carbon-limited (C-limited) or magnesium-limited (Mg-limited) conditions where teichoic acid predominated in the cell wall. However, the cell wall composition was not of significance in protein export and the parameters for the excretion process were found to be environmental. In particular, two types of extracellular proteins were identified: the first type of enzyme, penicillinase, was only weakly catabolite repressed; was maximally synthesized and secreted during P-limited growth; was unaffected by growth in high Na+ media but its production was inhibited by gramicidin. The second type of enzyme, α-amylase, was strongly catabolite repressed and its export was markedly inhibited during P-limited growth or in the presence of Na+ or gramicidin. It is noteworthy that the penicillinase carries a glyceride-cysteine modification at its N-terminus whilst the α-amylase does not.

Key words

Bacillus licheniformis Teichoic and teichuronic acids Protein export Na+ and gramidicin inhibition 
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References

  1. Chen PS Jr, Tobibara TY, Warner H (1956) Microdetermination of phosphorus. Anal Chem 28:1756–1758Google Scholar
  2. Daniels CJ, Bole DG, Quay SC, Oxender DL (1981) Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli. Proc Natl Acad Sci USA 78:5396–5400Google Scholar
  3. Dische Z (1947) A new specific colour reaction for hexuronic acids. J Biol Chem 167:189–198Google Scholar
  4. Ellwood DC, Tempest DW (1969) Control of teichoic acid and teichuronic acid biosynthesis in chemostat cultures of Bacillus subtilis var niger. Biochem J 111:1–5Google Scholar
  5. Ellwood DC, Tempest DW (1972) Effects of environment on bacterial wall content and composition. Adv Microbiol Physiol 7:83–117Google Scholar
  6. Forsberg CW, Wyrick PB, Ward JB, Rogers HJ (1973) Effect of phosphate limitation on the morphology and wall composition of Bacillus licheniformis and its phosphoglucomutase-deficient mutants. J Bacteriol 113:969–984Google Scholar
  7. Keevil CW, Hamilton IR (1984) Comparison of polyvinyl chloride membrane electrodes sensitive to alkylphosphonium ions for the determination of the electrical difference (Δψ) of Streptococcus mutants and Lactobacillus casei. Anal Biochem 139:228–236Google Scholar
  8. Keevil CW, West AA, Bourne N, Marsh PD (1984) Inhibition of the synthesis and secretion of extracellular glucosyl-and fructosyltransferase in Streptococcus sanguis by sodium ions. J Gen Microbiol 130:77–82Google Scholar
  9. Kuhn H, Fietzek PP, Lampen JO (1982) N-terminal amino acid sequence of Bacillus licheniformis α-amylase: Comparison with Bacillus amyloliquefaciens and Bacillus subtilis enzymes. J Bacteriol 149:372–373Google Scholar
  10. Mäntsälä P, Lehtinen H (1982) Secretion of β-lactamase by Escherichia coli in vivo and in vitro: effect of cerulenin. Antonie von Leeuwenhoek J Microbiol Serol 48:353–364Google Scholar
  11. Mäntsälä P, Zalkin H (1979) Membrane-bound and soluble extracellular-amylase from Bacillus subtilis. J Biol Chem 254:8540–8547Google Scholar
  12. Meers JL (1972) The regulation of α-amylase production in bacillus licheniformis. Antonie van Leeuwenhoek J Microbiol Serol 38:585–590Google Scholar
  13. Nielsen JBK, Lampen JO (1982) Membrane-bound penicillinases in Gram-positive bacteria. J Biol Chem 257:4490–4495Google Scholar
  14. Osborn MJ, Gander JE, Parisi E, Carson J (1972) Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem 247:3962–3972Google Scholar
  15. O'Callaghan CH, Morris A, Kirby S, Shingler AH (1972) Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother 1:283–288Google Scholar
  16. Pages JM, Lazdunski C (1982) Membrane potential (Δψ) depolarising agents inhibit maturation. FEBS Lett 149:51–54Google Scholar
  17. Street HV (1974) Alpha-amylase: Measurement of the starch-iodine complex. Methods Enz Anal 2:898–903Google Scholar
  18. Tempest DW, Dicks JW, Ellwood DC (1968) Influence of growth condition on the concentration of potassium in Bacillus subtilis var niger and its possible relationship to cellular ribonucleic acid, teichoc acid and teichuronic acid. Biochem J 106:237–243Google Scholar
  19. West AA, Keevil CW, Marsh PD, Ellwood DC (1984) The effect of ionophores on growth and glycosyltransferase production of Streptococcus sanguis. FEMS Microbiol Lett 25:133–137Google Scholar

Copyright information

© Springer-Verlag 1987

Authors and Affiliations

  • M. J. Lancaster
    • 1
  • C. W. Keevil
    • 2
  • D. C. Ellwood
    • 2
  • R. C. W. Berkeley
    • 1
  1. 1.Department of Microbiology, The Medical SchoolUniversity of BristolBristolUK
  2. 2.Pathogenic Microbes Research LaboratoryPHLS Centre for Applied Microbiology and ResearchSallsburyUK

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