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.
MeSH Terms
Amino Acid Sequence
Bacterial Proteins/genetics
Bacteriolysis
Base Sequence
Biological Transport
Cell Compartmentation
Enterococcus/genetics,metabolism
Genes, Bacterial
Genetic Complementation Test
Molecular Sequence Data
Muramidase/metabolism
Mutagenesis
Sequence Analysis, DNA
Sequence Deletion
Chemicals
Bacterial Proteins
arpU protein, Enterococcus hirae
Muramidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lleò M M
Institute of Microbiology, University of Verona, Italy.
Fontana R
Solioz M
References (21)
21 references, click to expand
-
The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo.
J Gen Microbiol. 1991 Mar;137(3):441-54
PMID: 1674525
-
Purification and properties of a germination-specific cortex-lytic enzyme from spores of Bacillus megaterium KM.
Biochem J. 1987 Mar 1;242(2):573-9
PMID: 3109395
-
A simple method for displaying the hydropathic character of a protein.
J Mol Biol. 1982 May 5;157(1):105-32
PMID: 7108955
-
Improved medium for lactic streptococci and their bacteriophages.
Appl Microbiol. 1975 Jun;29(6):807-13
PMID: 16350018
-
The autolytic peptidoglycan hydrolases of Streptococcus faecium.
Ann Inst Pasteur Microbiol. 1985 Jan-Feb;136A(1):63-6
PMID: 2860842
-
Efficient electrotransformation of Enterococcus hirae with a new Enterococcus-Escherichia coli shuttle vector.
Biochimie. 1990 Apr;72(4):279-83
PMID: 2116916
-
Morphological and physiological study of autolytic-defective Streptococcus faecium strains.
J Bacteriol. 1979 May;138(2):598-608
PMID: 108262
-
Simple and rapid method for isolating large plasmid DNA from lactic streptococci.
Appl Environ Microbiol. 1983 Sep;46(3):549-52
PMID: 6416164
-
Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis.
Can J Microbiol. 1989 Aug;35(8):749-53
PMID: 2819603
-
The mechanism of soluble peptidoglycan hydrolysis by an autolytic muramidase. A processive exodisaccharidase.
J Biol Chem. 1984 Oct 10;259(19):11818-27
PMID: 6480585
-
The complete general secretory pathway in gram-negative bacteria.
Microbiol Rev. 1993 Mar;57(1):50-108
PMID: 8096622
-
A comprehensive set of sequence analysis programs for the VAX.
Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387-95
PMID: 6546423
-
Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae.
J Bacteriol. 1992 Mar;174(5):1619-25
PMID: 1347040
-
Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin.
FEMS Microbiol Lett. 1992 Mar 15;70(3):257-64
PMID: 1352512
-
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):314-20
PMID: 2109578
-
Relations between bacterial cell wall synthesis, growth phase, and autolysis.
J Biol Chem. 1958 Feb;230(2):961-77
PMID: 13525413
-
Some properties of two autolytic-defective mutants of Streptococcus faecalis ATCC 9790.
J Bacteriol. 1972 Jan;109(1):423-31
PMID: 4109890
-
Isolation and characterization of autolysis-defective mutants of Staphylococcus aureus created by Tn917-lacZ mutagenesis.
J Bacteriol. 1993 Mar;175(5):1493-9
PMID: 8095258
-
The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin.
J Bacteriol. 1989 Aug;171(8):4355-61
PMID: 2753858
-
Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme.
J Biol Chem. 1983 Aug 10;258(15):9514-21
PMID: 6874701
-
Isolation and characterization of a Tn551-autolysis mutant of Staphylococcus aureus.
J Bacteriol. 1992 Aug;174(15):4952-9
PMID: 1321119