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Volumn 181, Issue 15, 1999, Pages 4452-4460

Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; HYDROLASE; PEPTIDOGLYCAN;

EID: 0032809133     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.15.4452-4460.1999     Document Type: Article
Times cited : (75)

References (46)
  • 2
    • 0028357986 scopus 로고
    • Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins
    • Arendt, E. K., C. Daly, G. F. Fitzgerald, and M. van de Guchte. 1994. Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins. Appl. Environ. Microbiol. 60:1875-1883.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1875-1883
    • Arendt, E.K.1    Daly, C.2    Fitzgerald, G.F.3    Van De Guchte, M.4
  • 3
    • 0344251978 scopus 로고
    • The effect of heat on the ability of a host strain to support the growth of a Staphylococcus phage
    • Asheshov, E. A., and M. P. Jevons. 1963. The effect of heat on the ability of a host strain to support the growth of a Staphylococcus phage. J. Gen. Microbiol. 31:97-107.
    • (1963) J. Gen. Microbiol. , vol.31 , pp. 97-107
    • Asheshov, E.A.1    Jevons, M.P.2
  • 4
    • 0029790464 scopus 로고    scopus 로고
    • Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus
    • Baba, T., and O. Schneewind. 1996. Target cell specificity of a bacteriocin molecule: a C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus. EMBO J. 15:4789-4797.
    • (1996) EMBO J. , vol.15 , pp. 4789-4797
    • Baba, T.1    Schneewind, O.2
  • 5
    • 0030861340 scopus 로고    scopus 로고
    • The Serratia marcescens NucE protein functions as a holin in Escherichia coli
    • Berkmen, M., M. J. Benedik, and U. Bläsi. 1997. The Serratia marcescens NucE protein functions as a holin in Escherichia coli. J. Bacteriol. 179:6522-6524.
    • (1997) J. Bacteriol. , vol.179 , pp. 6522-6524
    • Berkmen, M.1    Benedik, M.J.2    Bläsi, U.3
  • 6
    • 0027981084 scopus 로고
    • Cloning, molecular characterization, and expression of the genes encoding lytic functions of lactococcal bacteriophage φLC3: A dual lysis system of modular design
    • Birkeland, N.-K. 1994. Cloning, molecular characterization, and expression of the genes encoding lytic functions of lactococcal bacteriophage φLC3: a dual lysis system of modular design. Can. J. Microbiol. 40:658-665.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 658-665
    • Birkeland, N.-K.1
  • 7
  • 8
    • 0029764787 scopus 로고    scopus 로고
    • Two beginnings for a single purpose: The dual-start holins in the regulation of phage lysis
    • Bläsi, U., and R. Young. 1996. Two beginnings for a single purpose: the dual-start holins in the regulation of phage lysis. Mol. Microbiol. 21:675-682.
    • (1996) Mol. Microbiol. , vol.21 , pp. 675-682
    • Bläsi, U.1    Young, R.2
  • 9
    • 0029020763 scopus 로고
    • S gene expression and timing of lysis by bacteriophage λ
    • Chang, C.-Y., K. Nam, and R. Young. 1995. S gene expression and timing of lysis by bacteriophage λ. J. Bacteriol. 177:3283-3294.
    • (1995) J. Bacteriol. , vol.177 , pp. 3283-3294
    • Chang, C.-Y.1    Nam, K.2    Young, R.3
  • 10
    • 0030028470 scopus 로고    scopus 로고
    • The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram negative bacteria: Triggering of the major pneumococcal autolysin in E. coli
    • Diaz, E., M. Munthali, H. Lünsdorf, J.-V. Höltje, and K. N. Timmis. 1996. The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram negative bacteria: triggering of the major pneumococcal autolysin in E. coli. Mol. Microbiol. 19:667-681.
    • (1996) Mol. Microbiol. , vol.19 , pp. 667-681
    • Diaz, E.1    Munthali, M.2    Lünsdorf, H.3    Höltje, J.-V.4    Timmis, K.N.5
  • 11
    • 0029617205 scopus 로고
    • Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4
    • Foster, S. J. 1995. Molecular characterization and functional analysis of the major autolysin of Staphylococcus aureus 8325/4. J. Bacteriol. 177:5723-5725.
    • (1995) J. Bacteriol. , vol.177 , pp. 5723-5725
    • Foster, S.J.1
  • 13
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • García, P., J. L. García, J. M. García, J. M. Sánchez-Puelles, and R. López. 1990. Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86:137-142.
    • (1990) Gene , vol.86 , pp. 137-142
    • García, P.1    García, J.L.2    García, J.M.3    Sánchez-Puelles, J.M.4    López, R.5
  • 14
    • 0027236950 scopus 로고
    • Expression of the Rz gene and the overlapping Rz1 reading frame present at the right end of the bacteriophage lambda genome
    • Hanych, B., S. Kedzierska, B. Walderich, B. Uznanski, and A. Taylor. 1993. Expression of the Rz gene and the overlapping Rz1 reading frame present at the right end of the bacteriophage lambda genome. Gene 129:1-8.
    • (1993) Gene , vol.129 , pp. 1-8
    • Hanych, B.1    Kedzierska, S.2    Walderich, B.3    Uznanski, B.4    Taylor, A.5
  • 15
    • 0030798156 scopus 로고    scopus 로고
    • Evidence for autolysin-mediated primary attachment of Staphylococcus epidemidis to a polystyrene surface
    • Heilmann, C., M. Hussain, G. Peters, and F. Götz. 1997. Evidence for autolysin-mediated primary attachment of Staphylococcus epidemidis to a polystyrene surface. Mol. Microbiol. 24:1013-1024.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1013-1024
    • Heilmann, C.1    Hussain, M.2    Peters, G.3    Götz, F.4
  • 16
    • 0023429365 scopus 로고
    • The molecular organization of the lysostaphin gene and its sequences repeated in tandem
    • Heinrich, P., R. Rosenstein, M. Böhmer, P. Sonner, and F. Götz. 1987. The molecular organization of the lysostaphin gene and its sequences repeated in tandem. Mol. Gen. Genet. 209:563-569.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 563-569
    • Heinrich, P.1    Rosenstein, R.2    Böhmer, M.3    Sonner, P.4    Götz, F.5
  • 17
    • 0028954627 scopus 로고
    • Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage φadh
    • Henrich, B., B. Binishofer, and U. Bläsi. 1995. Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage φadh. J. Bacteriol. 177:723-732.
    • (1995) J. Bacteriol. , vol.177 , pp. 723-732
    • Henrich, B.1    Binishofer, B.2    Bläsi, U.3
  • 19
    • 0342655941 scopus 로고    scopus 로고
    • The Rz gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli
    • Kedzierska, S., A. Wawrzynow, and A. Taylor. 1996. The Rz gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli. Gene 168:1-8.
    • (1996) Gene , vol.168 , pp. 1-8
    • Kedzierska, S.1    Wawrzynow, A.2    Taylor, A.3
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolitle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolitle, R.F.2
  • 21
    • 0022181510 scopus 로고
    • The virion proteins and ultrastructure of Staphylococcus aureus bacteriophages
    • Lee, J. S., and P. R. Stewart. 1985. The virion proteins and ultrastructure of Staphylococcus aureus bacteriophages. J. Gen. Virol. 66:2017-2027.
    • (1985) J. Gen. Virol. , vol.66 , pp. 2017-2027
    • Lee, J.S.1    Stewart, P.R.2
  • 22
    • 0032525314 scopus 로고    scopus 로고
    • The two-component lysis system of Staphylococcus aureus bacteriophage Twort: A large TTG-start holin and an associated amidase endolysin
    • Loessner, M. J., S. Gaeng, G. Wendlinger, S. K. Maier, and S. Scherer. 1998. The two-component lysis system of Staphylococcus aureus bacteriophage Twort: a large TTG-start holin and an associated amidase endolysin. FEMS Microbiol. Lett. 162:265-274.
    • (1998) FEMS Microbiol. Lett. , vol.162 , pp. 265-274
    • Loessner, M.J.1    Gaeng, S.2    Wendlinger, G.3    Maier, S.K.4    Scherer, S.5
  • 23
    • 0030894847 scopus 로고    scopus 로고
    • Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli
    • Loessner, M. J., S. K. Maier, H. Daubek-Puza, G. Wendlinger, and S. Scherer. 1997. Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli. J. Bacteriol. 179:2845-2851.
    • (1997) J. Bacteriol. , vol.179 , pp. 2845-2851
    • Loessner, M.J.1    Maier, S.K.2    Daubek-Puza, H.3    Wendlinger, G.4    Scherer, S.5
  • 24
    • 0029122651 scopus 로고
    • Heterogeneous endolysins in Listeria monocytogenes bacteriophages: A new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes
    • Loessner, M. J., G. Wendlinger, and S. Scherer. 1995. Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes. Mol. Microbiol. 16:1231-1241.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1231-1241
    • Loessner, M.J.1    Wendlinger, G.2    Scherer, S.3
  • 25
    • 0028131141 scopus 로고
    • Lytic enzymes associated with defective prophages of Bacillus subtilis: Sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX
    • Longchamp, P. F., C. Mauël, and D. Karamata. 1994. Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX. Microbiology 140:1855-1867.
    • (1994) Microbiology , vol.140 , pp. 1855-1867
    • Longchamp, P.F.1    Mauël, C.2    Karamata, D.3
  • 27
    • 0031912599 scopus 로고    scopus 로고
    • Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells
    • Martín, A. C., R. Löpez, and P. García. 1998. Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells. J. Bacteriol. 180:210-217.
    • (1998) J. Bacteriol. , vol.180 , pp. 210-217
    • Martín, A.C.1    Löpez, R.2    García, P.3
  • 28
    • 0019811426 scopus 로고
    • Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus β-lactamase gene
    • McLaughlin, J. R., C. L. Murray, and J. C. Rabinowitz. 1981. Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus β-lactamase gene. J. Biol. Chem. 256:11283-11291.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11283-11291
    • McLaughlin, J.R.1    Murray, C.L.2    Rabinowitz, J.C.3
  • 29
    • 0016140217 scopus 로고
    • Cellular antigens of staphylococci
    • Oeding, P. 1974. Cellular antigens of staphylococci. Ann. N.Y. Acad. Sci. 236:15-21.
    • (1974) Ann. N.Y. Acad. Sci. , vol.236 , pp. 15-21
    • Oeding, P.1
  • 30
    • 0028908856 scopus 로고
    • A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: Cloning, sequence analysis and characterization
    • Oshida, T., M. Sugai, H. Komatsuzawa, Y.-M. Hong, H. Suginaka, and A. Tomasz. 1995. A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis and characterization. Proc. Natl. Acad. Sci. USA 92:285-289.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 285-289
    • Oshida, T.1    Sugai, M.2    Komatsuzawa, H.3    Hong, Y.-M.4    Suginaka, H.5    Tomasz, A.6
  • 31
    • 0023100786 scopus 로고
    • Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans
    • Recsei, P. A., A. D. Gruss, and R. P. Novick. 1987. Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans. Proc. Natl. Acad. Sci. USA 84:1127-1131.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1127-1131
    • Recsei, P.A.1    Gruss, A.D.2    Novick, R.P.3
  • 32
    • 0030851313 scopus 로고    scopus 로고
    • The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactions
    • Rietsch, A., P. Fraisl, A. Grasschopf, and U. Bläsi. 1997. The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactions. FEMS Microbiol. Lett. 153:393-398.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 393-398
    • Rietsch, A.1    Fraisl, P.2    Grasschopf, A.3    Bläsi, U.4
  • 34
    • 0023472472 scopus 로고
    • Tricine sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-397.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-397
    • Schägger, H.1    Von Jagow, G.2
  • 35
    • 0030824227 scopus 로고    scopus 로고
    • The lytic enzyme of the pneumococcal phage Dp-1: A chimeric lysin of intergeneric origin
    • Sheehan, M. M., J. L. Garcia, R. López, and P. Garcia. 1997. The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. Mol. Microbiol. 25:717-725.
    • (1997) Mol. Microbiol. , vol.25 , pp. 717-725
    • Sheehan, M.M.1    Garcia, J.L.2    López, R.3    Garcia, P.4
  • 36
    • 0027211113 scopus 로고
    • Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105
    • Steiner, M., and U. Bläsi. 1993. Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105. Mol. Microbiol. 8:525-533.
    • (1993) Mol. Microbiol. , vol.8 , pp. 525-533
    • Steiner, M.1    Bläsi, U.2
  • 37
    • 0027528507 scopus 로고
    • The missing link in phage lysis of gram-positive bacteria: Gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein
    • Steiner, M., W. Lubitz, and U. Bläsi. 1993. The missing link in phage lysis of gram-positive bacteria: gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein. J. Bacteriol. 175:1038-1042.
    • (1993) J. Bacteriol. , vol.175 , pp. 1038-1042
    • Steiner, M.1    Lubitz, W.2    Bläsi, U.3
  • 38
    • 0028986933 scopus 로고
    • Identification of endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus
    • Sugai, M., H. Komatsuzawa, T. Akiyama, Y.-M. Hong, T. Oshida, Y. Miyake, T. Yamaguchi, and H. Suginaka. 1995. Identification of endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus. J. Bacteriol. 177:1491-1496.
    • (1995) J. Bacteriol. , vol.177 , pp. 1491-1496
    • Sugai, M.1    Komatsuzawa, H.2    Akiyama, T.3    Hong, Y.-M.4    Oshida, T.5    Miyake, Y.6    Yamaguchi, T.7    Suginaka, H.8
  • 41
    • 0028799370 scopus 로고
    • Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin
    • Vasala, A., M. Välkkila, J. Caldentey, and T. Alatossava. 1995. Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin. Appl. Environ. Microbiol. 61:4004-4011.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4004-4011
    • Vasala, A.1    Välkkila, M.2    Caldentey, J.3    Alatossava, T.4
  • 42
    • 0025778673 scopus 로고
    • Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity
    • Wang, X., B. J. Wilkinson, and R. K. Jayaswal. 1991. Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Gene 102:105-109.
    • (1991) Gene , vol.102 , pp. 105-109
    • Wang, X.1    Wilkinson, B.J.2    Jayaswal, R.K.3
  • 43
    • 0028882367 scopus 로고
    • Sequence analysis of the region upstream of a peptidoglycan hydrolase-encoding gene from bacteriophage φ11 of Staphylococcus aureus
    • Weerakoon, L. K., and R. K. Jayaswal. 1995. Sequence analysis of the region upstream of a peptidoglycan hydrolase-encoding gene from bacteriophage φ11 of Staphylococcus aureus. FEMS Microbiol. Lett. 133:9-15.
    • (1995) FEMS Microbiol. Lett. , vol.133 , pp. 9-15
    • Weerakoon, L.K.1    Jayaswal, R.K.2
  • 44
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • Young, R. 1992. Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56:430-481.
    • (1992) Microbiol. Rev. , vol.56 , pp. 430-481
    • Young, R.1
  • 45
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young, R., and U. Bläsi. 1995. Holins: form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 191-205
    • Young, R.1    Bläsi, U.2
  • 46
    • 0026500941 scopus 로고
    • Classification of virulent and temperate bacteriophages of Listeria spp. on the basis of morphology and protein analysis
    • Zink, R., and M. J. Loessner. 1992. Classification of virulent and temperate bacteriophages of Listeria spp. on the basis of morphology and protein analysis. Appl. Environ. Microbiol. 58:296-302.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 296-302
    • Zink, R.1    Loessner, M.J.2


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