Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1995 Oct;177(20):5912–5917. doi: 10.1128/jb.177.20.5912-5917.1995

Identification of a gene (arpU) controlling muramidase-2 export in Enterococcus hirae.

M M Lleò 1, R Fontana 1, M Solioz 1
PMCID: PMC177418  PMID: 7592343

Abstract

Muramidase-2 of Enterococcus hirae is a 74-kDa peptidoglycan hydrolase that plays a role in cell wall growth and division. To study its regulation, we isolated a mutant defective in muramidase-2 release under certain growth conditions. This mutant had cell walls which apparently lacked 74-kDa muramidase-2 but which accumulated two proteolytic fragments of 32 and 43 kDa, which exhibited muramidase-2 activity in the membrane fraction. By complementation cloning, we identified a 2.6-kb fragment of the E. hirae chromosome containing a gene cluster coding for proteins of 58 to 137 amino acids. One of these genes (arpU), which encoded a 15.9-kDa protein, was shown to complement the defect of the A9 mutant in trans. We propose that this gene may be involved in the regulation of muramidase-2 export.

Full Text

The Full Text of this article is available as a PDF (497.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson D. G., McKay L. L. Simple and rapid method for isolating large plasmid DNA from lactic streptococci. Appl Environ Microbiol. 1983 Sep;46(3):549–552. doi: 10.1128/aem.46.3.549-552.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barrett J. F., Dolinger D. L., Schramm V. L., Shockman G. D. The mechanism of soluble peptidoglycan hydrolysis by an autolytic muramidase. A processive exodisaccharidase. J Biol Chem. 1984 Oct 10;259(19):11818–11827. [PubMed] [Google Scholar]
  3. Chu C. P., Kariyama R., Daneo-Moore L., Shockman G. D. Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae. J Bacteriol. 1992 Mar;174(5):1619–1625. doi: 10.1128/jb.174.5.1619-1625.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dolinger D. L., Daneo-Moore L., Shockman G. D. The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J Bacteriol. 1989 Aug;171(8):4355–4361. doi: 10.1128/jb.171.8.4355-4361.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fontana R., Boaretti M., Grossato A., Tonin E. A., Lleò M. M., Satta G. Paradoxical response of Enterococcus faecalis to the bactericidal activity of penicillin is associated with reduced activity of one autolysin. Antimicrob Agents Chemother. 1990 Feb;34(2):314–320. doi: 10.1128/aac.34.2.314. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Foster S. J., Johnstone K. Purification and properties of a germination-specific cortex-lytic enzyme from spores of Bacillus megaterium KM. Biochem J. 1987 Mar 1;242(2):573–579. doi: 10.1042/bj2420573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Höltje J. V., Tuomanen E. I. The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo. J Gen Microbiol. 1991 Mar;137(3):441–454. doi: 10.1099/00221287-137-3-441. [DOI] [PubMed] [Google Scholar]
  9. Joris B., Englebert S., Chu C. P., Kariyama R., Daneo-Moore L., Shockman G. D., Ghuysen J. M. Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin. FEMS Microbiol Lett. 1992 Mar 15;70(3):257–264. doi: 10.1016/0378-1097(92)90707-u. [DOI] [PubMed] [Google Scholar]
  10. Kawamura T., Shockman G. D. Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme. J Biol Chem. 1983 Aug 10;258(15):9514–9521. [PubMed] [Google Scholar]
  11. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  12. Leclerc D., Asselin A. Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis. Can J Microbiol. 1989 Aug;35(8):749–753. doi: 10.1139/m89-125. [DOI] [PubMed] [Google Scholar]
  13. Mani N., Tobin P., Jayaswal R. K. Isolation and characterization of autolysis-defective mutants of Staphylococcus aureus created by Tn917-lacZ mutagenesis. J Bacteriol. 1993 Mar;175(5):1493–1499. doi: 10.1128/jb.175.5.1493-1499.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Oshida T., Tomasz A. Isolation and characterization of a Tn551-autolysis mutant of Staphylococcus aureus. J Bacteriol. 1992 Aug;174(15):4952–4959. doi: 10.1128/jb.174.15.4952-4959.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pooley H. M., Shockman G. D., Higgins M. L., Porres-Juan J. Some properties of two autolytic-defective mutants of Streptococcus faecalis ATCC 9790. J Bacteriol. 1972 Jan;109(1):423–431. doi: 10.1128/jb.109.1.423-431.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pugsley A. P. The complete general secretory pathway in gram-negative bacteria. Microbiol Rev. 1993 Mar;57(1):50–108. doi: 10.1128/mr.57.1.50-108.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. SHOCKMAN G. D., KOLB J. J., TOENNIES G. Relations between bacterial cell wall synthesis, growth phase, and autolysis. J Biol Chem. 1958 Feb;230(2):961–977. [PubMed] [Google Scholar]
  18. Shockman G. D., Kawamura T., Barrett J. F., Dolinger D. L. The autolytic peptidoglycan hydrolases of Streptococcus faecium. Ann Inst Pasteur Microbiol. 1985 Jan-Feb;136A(1):63–66. doi: 10.1016/s0769-2609(85)80023-5. [DOI] [PubMed] [Google Scholar]
  19. Shungu D. L., Cornett J. B., Shockman G. D. Morphological and physiological study of autolytic-defective Streptococcus faecium strains. J Bacteriol. 1979 May;138(2):598–608. doi: 10.1128/jb.138.2.598-608.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Solioz M., Waser M. Efficient electrotransformation of Enterococcus hirae with a new Enterococcus-Escherichia coli shuttle vector. Biochimie. 1990 Apr;72(4):279–283. doi: 10.1016/0300-9084(90)90084-t. [DOI] [PubMed] [Google Scholar]
  21. Terzaghi B. E., Sandine W. E. Improved medium for lactic streptococci and their bacteriophages. Appl Microbiol. 1975 Jun;29(6):807–813. doi: 10.1128/am.29.6.807-813.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES