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Volumn 168, Issue 1, 1996, Pages 1-8

The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli

Author keywords

Bacterial lysis; Bacterial membrane adhesion site; Globomycin; Immunodetection; Overlapping Rz Rz1 genes; Proline rich protein; Rz1 prolipoprotein; Synthetic immuno determinant

Indexed keywords

GENE PRODUCT; LIPOPROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0342655941     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(95)00712-1     Document Type: Article
Times cited : (43)

References (32)
  • 1
    • 0019781647 scopus 로고
    • The R gene product of bacteriophage λ is the murein transglycosylase
    • Bieńkowska-Szewczyk, K., Lipińska, B. and Taylor, A.: The R gene product of bacteriophage λ is the murein transglycosylase. Mol. Gen. Genet. 184 (1981) 111-114.
    • (1981) Mol. Gen. Genet. , vol.184 , pp. 111-114
    • Bieńkowska-Szewczyk, K.1    Lipińska, B.2    Taylor, A.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M.: A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.M.1
  • 3
    • 77956860575 scopus 로고
    • Lipoproteins, structure, function, biosynthesis and model for protein export
    • Ghuysen, J.-M. and Hakenbeck, R. (Eds.), Elsevier, New York, NY
    • Braun, V. and Wu, H.C.: Lipoproteins, structure, function, biosynthesis and model for protein export. In: Ghuysen, J.-M. and Hakenbeck, R. (Eds.), Bacterial Cell Wall. Elsevier, New York, NY, 1994, pp. 319-341.
    • (1994) Bacterial Cell Wall , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 4
    • 0001740960 scopus 로고
    • Mutant of bacteriophage lambda producing a thermolabile endolysin
    • Campbell, A. and Campillo-Campbell, A.D.: Mutant of bacteriophage lambda producing a thermolabile endolysin. J. Bacteriol. 85 (1963) 1202-1207.
    • (1963) J. Bacteriol. , vol.85 , pp. 1202-1207
    • Campbell, A.1    Campillo-Campbell, A.D.2
  • 5
    • 0343089427 scopus 로고
    • Production of antipeptide antibodies
    • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.), Harvard Medical School, Boston, MA
    • Collawn, J.F. and Paterson, Y.: Production of antipeptide antibodies. In: Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (Eds.), Current Protocols in Molecular Biology. Harvard Medical School, Boston, MA, 1989, pp.11.15.2-11.15.3.
    • (1989) Current Protocols in Molecular Biology , pp. 11152-11153
    • Collawn, J.F.1    Paterson, Y.2
  • 6
    • 0021800753 scopus 로고
    • Inhibition of prolipoprotein signal peptidase by globomycin
    • Dev, I.K., Harvey, R.J. and Ray, P.H.: Inhibition of prolipoprotein signal peptidase by globomycin. J. Biol. Chem. 260 (1985) 5891-5894.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5891-5894
    • Dev, I.K.1    Harvey, R.J.2    Ray, P.H.3
  • 7
    • 0018860803 scopus 로고
    • Alterations in the cell envelope of Escherichia coli late in bacteriophage T4 infection
    • Fletcher, G. and Earhardt, C.F.: Alterations in the cell envelope of Escherichia coli late in bacteriophage T4 infection. Biochim. Biophys. Acta 596 (1980) 210-222.
    • (1980) Biochim. Biophys. Acta , vol.596 , pp. 210-222
    • Fletcher, G.1    Earhardt, C.F.2
  • 9
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch, L.M.: Signal sequences. Biochemistry 28 (1989) 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 10
    • 0027236950 scopus 로고
    • Expression of the Rz gene and overlapping Rz1 reading frame present at the right end of the bacteriophage λ genome
    • Hanych, B., Kȩdzierska, S., Walderich, B., Uznański, B. and Taylor, A.: Expression of the Rz gene and overlapping Rz1 reading frame present at the right end of the bacteriophage λ genome. Gene 129 (1993a) 1-8.
    • (1993) Gene , vol.129 , pp. 1-8
    • Hanych, B.1    Kȩdzierska, S.2    Walderich, B.3    Uznański, B.4    Taylor, A.5
  • 11
    • 0008933764 scopus 로고
    • Molecular cloning, overexpression of Rz lysis gene of phage λ and subcellular localization of its protein product
    • De Pedro, M., Höltje, J.V. and Löffelhardt, W. (Eds.), Plenum, New York, NY
    • Hanych, B., Kȩdzierska, S., Walderich, B. and Taylor, A.: Molecular cloning, overexpression of Rz lysis gene of phage λ and subcellular localization of its protein product. In: De Pedro, M., Höltje, J.V. and Löffelhardt, W. (Eds.), Bacterial Growth and Lysis: Metabolizm and Structure of the Bacterial Sacculus. Plenum, New York, NY, 1993b, pp. 269-276.
    • (1993) Bacterial Growth and Lysis: Metabolizm and Structure of the Bacterial Sacculus , pp. 269-276
    • Hanych, B.1    Kȩdzierska, S.2    Walderich, B.3    Taylor, A.4
  • 14
    • 0017610608 scopus 로고
    • On the process of cellular division in Escherichia coli: A mutant of E. coli lacking a murein-lipoprotein
    • Hirota, Y., Suzuki, H., Nishimura, Y. and Yasuda, S.: On the process of cellular division in Escherichia coli: a mutant of E. coli lacking a murein-lipoprotein. Proc. Natl. Acad. Sci. USA 74 (1977) 1417-1420.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 1417-1420
    • Hirota, Y.1    Suzuki, H.2    Nishimura, Y.3    Yasuda, S.4
  • 16
    • 0022633653 scopus 로고
    • Isolation of differentiated membrane domains from Escherichiu coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope
    • Ishidate, K., Creeger, E.S., Zrike, J., Deb, S., Glauner, B., MacAlister, T.J. and Rothfield, L.I.: Isolation of differentiated membrane domains from Escherichiu coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope. J. Biol. Chem. 261 (1986) 428-443.
    • (1986) J. Biol. Chem. , vol.261 , pp. 428-443
    • Ishidate, K.1    Creeger, E.S.2    Zrike, J.3    Deb, S.4    Glauner, B.5    MacAlister, T.J.6    Rothfield, L.I.7
  • 17
    • 0026355680 scopus 로고
    • Response of Escherichia coli cell membranes to induction of λc1857 prophage by heat shock
    • Kucharczyk, K., Laskowska, L. and Taylor, A.: Response of Escherichia coli cell membranes to induction of λc1857 prophage by heat shock. Mol. Microbiol. 5 (1991) 2935-2945.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2935-2945
    • Kucharczyk, K.1    Laskowska, L.2    Taylor, A.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A.: The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57 (1993) 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 20
    • 0024278076 scopus 로고
    • Dominance in lambda s mutations and evidence for translational control
    • Raab, R., Neal, G., Shoaskey, Ch., Smith, J. and Young, R.: Dominance in lambda S mutations and evidence for translational control. J. Mol. Biol. 199 (1988) 95-105.
    • (1988) J. Mol. Biol. , vol.199 , pp. 95-105
    • Raab, R.1    Neal, G.2    Shoaskey, C.H.3    Smith, J.4    Young, R.5
  • 22
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of the cloned genes
    • Studier, F.W., Rosenberg, A,L., Dunn, J.J. and Dubendorf, J.W.: Use of T7 RNA polymerase to direct expression of the cloned genes. Methods Enzymol. 185 (1990) 60-89.
    • (1990) Methods Enzymol. , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.2    Dunn, J.J.3    Dubendorf, J.W.4
  • 23
    • 0023392871 scopus 로고
    • Fluorescent staining of proteins transferred to nitrocellulose allowing for subsequent probing with antisera
    • Szewczyk, B. and Summers, D.F.: Fluorescent staining of proteins transferred to nitrocellulose allowing for subsequent probing with antisera. Anal. Biochem. 164 (1987) 303-306.
    • (1987) Anal. Biochem. , vol.164 , pp. 303-306
    • Szewczyk, B.1    Summers, D.F.2
  • 24
    • 0015174355 scopus 로고
    • Endopeptidase activity of phage lambda endolysin
    • Taylor, A.: Endopeptidase activity of phage lambda endolysin. Nature New. Biol. 234 (1971) 144-145.
    • (1971) Nature New. Biol. , vol.234 , pp. 144-145
    • Taylor, A.1
  • 25
    • 0016396054 scopus 로고
    • Isolement and caracterisation de l'acide N-acetylglucosaminyl-β-1-4-1,6-anhydro-N-acetylmuramique
    • Taylor, A., Das, B. and Van Heijenoort, J.: Isolement and caracterisation de l'acide N-acetylglucosaminyl-β-1-4-1,6-anhydro-N-acetylmuramique. C.R. Acad. Sci. Paris 278 (1974) 1127-1129.
    • (1974) C.R. Acad. Sci. Paris , vol.278 , pp. 1127-1129
    • Taylor, A.1    Das, B.2    Van Heijenoort, J.3
  • 26
    • 0016669460 scopus 로고
    • Bacterial-cell-wall peptidoglycan fragments produced by phage lambda or Vi II endolysin and containing 1,6-anhydro-N-acetylmuramic acid
    • Taylor, A., Das, B.C. and Van Heijenoort, J.: Bacterial-cell-wall peptidoglycan fragments produced by phage lambda or Vi II endolysin and containing 1,6-anhydro-N-acetylmuramic acid. Eur. J. Biochem. 53 (1975) 47-54.
    • (1975) Eur. J. Biochem. , vol.53 , pp. 47-54
    • Taylor, A.1    Das, B.C.2    Van Heijenoort, J.3
  • 27
    • 0021070654 scopus 로고
    • Localization of Rz gene in bacteriophage lambda
    • Taylor, A., Benedik, M. and Campbell, A.: Localization of Rz gene in bacteriophage lambda. Gene 26 (1983) 159-163.
    • (1983) Gene , vol.26 , pp. 159-163
    • Taylor, A.1    Benedik, M.2    Campbell, A.3
  • 28
    • 0021770334 scopus 로고
    • How signal sequences maintain cleavage specificity
    • Von Heijne, G.: How signal sequences maintain cleavage specificity. J. Mol. Biol.173 (1984) 99-105.
    • (1984) J. Mol. Biol. , vol.173 , pp. 99-105
    • Von Heijne, G.1
  • 29
    • 0023734562 scopus 로고
    • Induction of the autolytic system of Escherichia coli by specific insertion of bacteriophage MS2 lysis protein into the bacterial cell envelope
    • Walderich, B., Ursinus-Wössner, A., Van Duin, J. and Höltje, J.-V.: Induction of the autolytic system of Escherichia coli by specific insertion of bacteriophage MS2 lysis protein into the bacterial cell envelope. J. Bacteriol. 170 (1988) 5027-5033.
    • (1988) J. Bacteriol. , vol.170 , pp. 5027-5033
    • Walderich, B.1    Ursinus-Wössner, A.2    Van Duin, J.3    Höltje, J.-V.4
  • 30
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M.P.: The structure and function of proline-rich regions in proteins. Biochem. J. 297 (1994) 249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 31
    • 0018791980 scopus 로고
    • Transposition mutagenesis of bacteriophage lambda. A new gene affecting cell lysis
    • Young, R., Way, J., Way, S., Yin, J. and Syvanen, M.: Transposition mutagenesis of bacteriophage lambda. A new gene affecting cell lysis. J. Mol. Biol. 132 (1979) 307-322.
    • (1979) J. Mol. Biol. , vol.132 , pp. 307-322
    • Young, R.1    Way, J.2    Way, S.3    Yin, J.4    Syvanen, M.5
  • 32
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • Young, R.: Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56 (1992) 430-481.
    • (1992) Microbiol. Rev. , vol.56 , pp. 430-481
    • Young, R.1


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