Abstract
The cellular localization of staphylococcus nuclease, previously known as an exoenzyme, was investigated, and the following results were obtained. (i) When Staphylococcus aureus cells were converted to protoplasts by cell wall lytic enzyme L-11 (a bacteriolytic enzyme purified from Flavobacterium sp. which specifically hydrolyzes amide and peptide linkages of murein layers), over 80% of the cell-bound nuclease was released into the surrounding sucrose medium. (ii) The cell-bound nuclease was associated with the cell-wall membrane fraction of mechanically disrupted cells. (iii) The nuclease activity of cell-wall membrane fractions from cells during early and late stages of protoplast formation were compared. Less activity was found in the late stage. These results suggest that nuclease may be located at or near the surface of the cells. The distribution of cell-bound nuclease in the cell-wall membrane fraction varied with the growth conditions of S. aureus. The activity of alkaline phosphatase, another surface enzyme, was also investigated. Less of this enzyme than nuclease was released when the cells were converted to protoplasts.
MeSH Terms
Alkaline Phosphatase/metabolism
Cell Fractionation
Cell Membrane/enzymology
Cell Wall/enzymology
Culture Media
DNA, Bacterial/metabolism
Deoxyribonucleases/isolation & purification,metabolism
Enzymes/metabolism
Escherichia coli
Flavobacterium/enzymology
L-Lactate Dehydrogenase/metabolism
Phosphates/metabolism
Protoplasts/enzymology
RNA, Bacterial/metabolism
RNA, Ribosomal/metabolism
Ribonucleases/isolation & purification,metabolism
Staphylococcus/enzymology,growth & development
Thymine/metabolism
Time Factors
Tritium
Uridine/metabolism
Chemicals
Culture Media
DNA, Bacterial
Enzymes
Phosphates
RNA, Bacterial
RNA, Ribosomal
Tritium
L-Lactate Dehydrogenase
Deoxyribonucleases
Ribonucleases
Alkaline Phosphatase
Thymine
Uridine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Okabayaski K
Mizuno D
References (26)
26 references, click to expand
-
Electron microscopic studies on the outer layers of Staphylococcus aureus using a lytic enzyme from Falvobacterium.
Jpn J Microbiol. 1972 Sep;16(5):341-50
PMID: 4539618
-
The localization of alkaline phosphatase in E. coli K12.
Biochem Biophys Res Commun. 1961 Jun 2;5:104-8
PMID: 13765699
-
The mechanism of liberation of penicillinase from Bacillus subtilis.
J Gen Microbiol. 1961 Oct;26:267-76
PMID: 14487666
-
Biochemical properties of virulent and avirulent staphylococci.
Ann N Y Acad Sci. 1960 Nov 21;88:1115-24
PMID: 13689191
-
Regulation of Staphylococcus aureus lactate dehydrogenase.
J Bacteriol. 1968 Jan;95(1):152-6
PMID: 4295239
-
Cellular site in Bacillus subtilis of a nuclease which preferentially degrades single-stranded nucleic acids.
J Bacteriol. 1966 Mar;91(3):1004-11
PMID: 4956329
-
THE DEOXYRIBONUCLEASES OF ESCHERICHIA COLI K12-LAMBDA.
J Biol Chem. 1963 Oct;238:3383-9
PMID: 14085391
-
Cytochemical localization of certain phosphatases in Escherichia coli.
J Bacteriol. 1970 Oct;104(1):529-42
PMID: 4319724
-
Selective release of enzymes from bacteria.
Science. 1967 Jun 16;156(3781):1451-5
PMID: 4304946
-
IMMUNOFLUORESCENT DEMONSTRATION OF CELL-ASSOCIATED STAPHYLOCOCCAL ENTEROTOXIN B.
J Bacteriol. 1965 Apr;89:1155
PMID: 14276112
-
Release of surface enzymes in Enterobacteriaceae by osmotic shock.
J Bacteriol. 1967 Dec;94(6):1934-45
PMID: 4294595
-
A new method for the isolation of ribonucleic acids from mammalian tissues.
Biochem J. 1956 Nov;64(3):405-8
PMID: 13373784
-
Cell-bound penicillinase of Bacillus licheniformis; properties and purification.
J Gen Microbiol. 1967 Aug;48(2):249-59
PMID: 6038893
-
PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT.
Biochim Biophys Acta. 1963 Aug 20;72:619-29
PMID: 14071565
-
The cell-bound penicillinase of Bacillus cereus.
J Gen Microbiol. 1956 Aug;15(1):154-69
PMID: 13357724
-
Surface-bound nuclease of Stapylococcus aureus: purification and properties of the enzymes.
J Bacteriol. 1974 Jan;117(1):222-6
PMID: 4808903
-
Localization of cell-bound penicillinase in Bacillus licheniformis.
J Bacteriol. 1968 Oct;96(4):1329-38
PMID: 4302175
-
Liberation of surface-located penicillinase from Staphylococcus aureus.
Biochem J. 1967 Mar;102(3):742-7
PMID: 16742488
-
The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts.
J Biol Chem. 1965 Sep;240(9):3685-92
PMID: 4284300
-
A RIBONUCLEASE FROM THE DEBRIS OF ESCHERICHIA COLI.
Biochem Biophys Res Commun. 1965 Feb 17;18:462-8
PMID: 14301444
-
Relationships among coagulase, enterotoxin, and heat-stable deoxyribonuclease production by Staphylococcus aureus.
Appl Microbiol. 1969 Jul;18(1):126-7
PMID: 4896099
-
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
PMID: 14907713
-
Immunofluorescent demonstration of staphylococcal leucocidin components F and S.
Br J Exp Pathol. 1968 Oct;49(5):477-95
PMID: 4178108
-
Degradation of ribosomal RNA in a temperature-sensitive Escherichia coli.
Arch Biochem Biophys. 1967 Feb;118(2):402-9
PMID: 5340500
-
Intracellular localization of deoxyribonucleases in Escherichia coli.
Biochim Biophys Acta. 1968 Jan 29;155(1):98-106
PMID: 4967316
-
The location of cell-bound penicillinase in Bacillus subtilis.
J Gen Microbiol. 1961 Oct;26:255-65
PMID: 14460899