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Volumn 192, Issue 3, 2010, Pages 725-733

The N-terminal transmembrane domain of λ S is required for holin but not antiholin function

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIHOLIN PROTEIN; HOLIN PROTEIN; LYSINE; METHIONINE; PROTEIN DERIVATIVE; S 105 PROTEIN; S 107 PROTEIN; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 75149113312     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01263-09     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0033043978 scopus 로고    scopus 로고
    • Characterization of the dual start motif of a class II holin gene
    • Barenboim, M., C. Y. Chang, F. dib Hajj, and R. Young. 1999. Characterization of the dual start motif of a class II holin gene. Mol. Microbiol. 32:715-727.
    • (1999) Mol. Microbiol , vol.32 , pp. 715-727
    • Barenboim, M.1    Chang, C.Y.2    dib Hajj, F.3    Young, R.4
  • 2
    • 0035933529 scopus 로고    scopus 로고
    • A protein antibiotic in the phage Qβ virion: Diversity in lysis targets
    • Bernhardt, T. G., I. N. Wang, D. K. Struck, and R. Young. 2001. A protein antibiotic in the phage Qβ virion: diversity in lysis targets. Science 292:2326-2329.
    • (2001) Science , vol.292 , pp. 2326-2329
    • Bernhardt, T.G.1    Wang, I.N.2    Struck, D.K.3    Young, R.4
  • 3
    • 0025317560 scopus 로고
    • The lethal λ S gene encodes its own inhibitor
    • Bläsi, U., C. Y. Chang, M. T. Zagotta, K. Nam, and R. Young. 1990. The lethal λ S gene encodes its own inhibitor. EMBO J. 9:981-989.
    • (1990) EMBO J , vol.9 , pp. 981-989
    • Bläsi, U.1    Chang, C.Y.2    Zagotta, M.T.3    Nam, K.4    Young, R.5
  • 4
    • 0024422744 scopus 로고
    • Dual translational initiation sites control function of the λ S gene
    • Bläsi, U., K. Nam, D. Hartz, L. Gold, and R. Young. 1989. Dual translational initiation sites control function of the λ S gene. EMBO J. 8:3501-3510.
    • (1989) EMBO J , vol.8 , pp. 3501-3510
    • Bläsi, U.1    Nam, K.2    Hartz, D.3    Gold, L.4    Young, R.5
  • 5
    • 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
  • 6
    • 0025854738 scopus 로고
    • Dual start motif in two lambdoid S genes unrelated to lambda S
    • Bonovich, M. T., and R. Young. 1991. Dual start motif in two lambdoid S genes unrelated to lambda S. J. Bacteriol. 173:2897-2905.
    • (1991) J. Bacteriol , vol.173 , pp. 2897-2905
    • Bonovich, M.T.1    Young, R.2
  • 7
    • 0029020763 scopus 로고
    • S gene expression and the timing of lysis by bacteriophage λ
    • Chang, C. Y., K. Nam, and R. Young. 1995. S gene expression and the 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
  • 9
    • 3042533402 scopus 로고    scopus 로고
    • Solubilization and delivery by GroEL of megadalton complexes of the lambda holin
    • Deaton, J., C. G. Savva, J. Sun, A. Holzenburg, J. Berry, and R. Young. 2004. Solubilization and delivery by GroEL of megadalton complexes of the lambda holin. Protein Sci. 13:1778-1786.
    • (2004) Protein Sci , vol.13 , pp. 1778-1786
    • Deaton, J.1    Savva, C.G.2    Sun, J.3    Holzenburg, A.4    Berry, J.5    Young, R.6
  • 10
    • 77957004481 scopus 로고
    • The rapid determination of amino groups with TNBS
    • Fields, R. 1972. The rapid determination of amino groups with TNBS. Methods Enzymol. 25:464-468.
    • (1972) Methods Enzymol , vol.25 , pp. 464-468
    • Fields, R.1
  • 11
    • 0344052661 scopus 로고    scopus 로고
    • Functional assembly of the lambda S holin requires periplasmic localization of its N-terminus
    • Graschopf, A., and U. Bläsi. 1999. Functional assembly of the lambda S holin requires periplasmic localization of its N-terminus. Arch. Microbiol. 172:31-39.
    • (1999) Arch. Microbiol , vol.172 , pp. 31-39
    • Graschopf, A.1    Bläsi, U.2
  • 12
    • 0032767883 scopus 로고    scopus 로고
    • Molecular function of the dual-start motif in the λ S holin
    • Graschopf, A., and U. Bläsi. 1999. Molecular function of the dual-start motif in the λ S holin. Mol. Microbiol. 33:569-582.
    • (1999) Mol. Microbiol , vol.33 , pp. 569-582
    • Graschopf, A.1    Bläsi, U.2
  • 13
    • 0342980358 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for three transmembrane domains in the class I holin, λ S
    • Gründling, A., U. Bläsi, and R. Young. 2000. Biochemical and genetic evidence for three transmembrane domains in the class I holin, λ S. J. Biol. Chem. 275:769-776.
    • (2000) J. Biol. Chem , vol.275 , pp. 769-776
    • Gründling, A.1    Bläsi, U.2    Young, R.3
  • 14
    • 0033758762 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of dimer and oligomer interactions of the λ S holin
    • Gründling, A., U. Bläsi, and R. Young. 2000. Genetic and biochemical analysis of dimer and oligomer interactions of the λ S holin. J. Bacteriol. 182:6082-6090.
    • (2000) J. Bacteriol , vol.182 , pp. 6082-6090
    • Gründling, A.1    Bläsi, U.2    Young, R.3
  • 16
    • 0033758938 scopus 로고    scopus 로고
    • Dimerization between the holin and holin inhibitor of phage lambda
    • Gründling, A., D. L. Smith, U. Bläsi, and R. Young. 2000. Dimerization between the holin and holin inhibitor of phage lambda. J. Bacteriol. 182:6075-6081.
    • (2000) J. Bacteriol , vol.182 , pp. 6075-6081
    • Gründling, A.1    Smith, D.L.2    Bläsi, U.3    Young, R.4
  • 17
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 0027984891 scopus 로고
    • A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype
    • Johnson-Boaz, R., C. Y. Chang, and R. Young. 1994. A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype. Mol. Microbiol. 13:495-504.
    • (1994) Mol. Microbiol , vol.13 , pp. 495-504
    • Johnson-Boaz, R.1    Chang, C.Y.2    Young, R.3
  • 19
    • 0019155698 scopus 로고
    • The origin of Q-independent derivatives of phage lambda
    • Kaiser, K. 1980. The origin of Q-independent derivatives of phage lambda. Mol. Gen. Genet. 179:547-554.
    • (1980) Mol. Gen. Genet , vol.179 , pp. 547-554
    • Kaiser, K.1
  • 21
    • 0014441360 scopus 로고
    • Deformylation and protein biosynthesis
    • Livingston, D. M., and P. Leder. 1969. Deformylation and protein biosynthesis. Biochemistry 8:435-443.
    • (1969) Biochemistry , vol.8 , pp. 435-443
    • Livingston, D.M.1    Leder, P.2
  • 22
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 23
    • 0025020274 scopus 로고
    • Conservation of a dual-start motif in P22 lysis gene regulation
    • Nam, K., U. Bläsi, M. T. Zagotta, and R. Young. 1990. Conservation of a dual-start motif in P22 lysis gene regulation. J. Bacteriol. 172:204-211.
    • (1990) J. Bacteriol , vol.172 , pp. 204-211
    • Nam, K.1    Bläsi, U.2    Zagotta, M.T.3    Young, R.4
  • 25
    • 0028604471 scopus 로고    scopus 로고
    • Powell, B. S., M. P. Rivas, D. L. Court, Y. Nakamura, and C. L. Turnbough, Jr. 1994. Rapid confirmation of single copy lambda prophage integration by PCR. Nucleic Acids Res. 22:5765-5766.
    • Powell, B. S., M. P. Rivas, D. L. Court, Y. Nakamura, and C. L. Turnbough, Jr. 1994. Rapid confirmation of single copy lambda prophage integration by PCR. Nucleic Acids Res. 22:5765-5766.
  • 26
    • 0024278076 scopus 로고
    • Dominance in lambda S mutations and evidence for translational control
    • Raab, R., G. Neal, C. Sohaskey, J. Smith, and R. Young. 1988. Dominance in lambda S mutations and evidence for translational control. J. Mol. Biol. 199:95-105.
    • (1988) J. Mol. Biol , vol.199 , pp. 95-105
    • Raab, R.1    Neal, G.2    Sohaskey, C.3    Smith, J.4    Young, R.5
  • 27
    • 0001267065 scopus 로고    scopus 로고
    • Characterization of cobalt (II)-substituted peptide deformylase: Function of the metal ion and the catalytic residue Glu-133
    • Rajagopalan, P. T., S. Grimme, and D. Pei. 2000. Characterization of cobalt (II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39:779-790.
    • (2000) Biochemistry , vol.39 , pp. 779-790
    • Rajagopalan, P.T.1    Grimme, S.2    Pei, D.3
  • 28
    • 0034893774 scopus 로고    scopus 로고
    • An ancient player unmasked: T4 rI encodes a t-specific antiholin
    • Ramanculov, E. R., and R. Young. 2001. An ancient player unmasked: T4 rI encodes a t-specific antiholin. Mol. Microbiol. 41:575-583.
    • (2001) Mol. Microbiol , vol.41 , pp. 575-583
    • Ramanculov, E.R.1    Young, R.2
  • 29
    • 0031923724 scopus 로고    scopus 로고
    • The λ holin accumulates beyond the lethal triggering concentration under hyper-expression conditions
    • Smith, D. L., C. Y. Chang, and R. Young. 1998. The λ holin accumulates beyond the lethal triggering concentration under hyper-expression conditions. Gene Expr. 7:39-52.
    • (1998) Gene Expr , vol.7 , pp. 39-52
    • Smith, D.L.1    Chang, C.Y.2    Young, R.3
  • 30
    • 0031957862 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the lambda holin
    • Smith, D. L., D. K. Struck, J. M. Scholtz, and R. Young. 1998. Purification and biochemical characterization of the lambda holin. J. Bacteriol. 180:2531-2540.
    • (1998) J. Bacteriol , vol.180 , pp. 2531-2540
    • Smith, D.L.1    Struck, D.K.2    Scholtz, J.M.3    Young, R.4
  • 31
    • 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
  • 32
    • 0014323081 scopus 로고
    • Protein chain initiation and deformylation in B. subtilis homogenates
    • Takeda, M., and R. E. Webster. 1968. Protein chain initiation and deformylation in B. subtilis homogenates. Proc. Natl. Acad. Sci. U. S. A. 60:1487-1494.
    • (1968) Proc. Natl. Acad. Sci. U. S. A , vol.60 , pp. 1487-1494
    • Takeda, M.1    Webster, R.E.2
  • 33
    • 35648978139 scopus 로고    scopus 로고
    • The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP
    • Tran, T. A., D. K. Struck, and R. Young. 2007. The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP. J. Bacteriol. 189:7618-7625.
    • (2007) J. Bacteriol , vol.189 , pp. 7618-7625
    • Tran, T.A.1    Struck, D.K.2    Young, R.3
  • 34
    • 25144505528 scopus 로고    scopus 로고
    • Periplasmic domains define holin-antiholin interactions in T4 lysis inhibition
    • Tran, T. A. T., D. K. Struck, and R. Young. 2005. Periplasmic domains define holin-antiholin interactions in T4 lysis inhibition. J. Bacteriol. 187:6631-6640.
    • (2005) J. Bacteriol , vol.187 , pp. 6631-6640
    • Tran, T.A.T.1    Struck, D.K.2    Young, R.3
  • 35
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 36
    • 0345269852 scopus 로고    scopus 로고
    • Functional regulation of the Listeria monocytogenes bacteriophage A118 holin by an intragenic inhibitor lacking the first transmembrane domain
    • Vukov, N., I. Moll, U. Bläsi, S. Scherer, and M. J. Loessner. 2003. Functional regulation of the Listeria monocytogenes bacteriophage A118 holin by an intragenic inhibitor lacking the first transmembrane domain. Mol. Microbiol. 48:173-186.
    • (2003) Mol. Microbiol , vol.48 , pp. 173-186
    • Vukov, N.1    Moll, I.2    Bläsi, U.3    Scherer, S.4    Loessner, M.J.5
  • 37
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang, I. N., D. L. Smith, and R. Young. 2000. Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54:799-825.
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 38
    • 0036132523 scopus 로고    scopus 로고
    • Bacteriophage holins: Deadly diversity
    • Young, R. 2002. Bacteriophage holins: deadly diversity. J. Mol. Microbiol. Biotechnol. 4:21-36.
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 21-36
    • Young, R.1
  • 39
    • 0034162940 scopus 로고    scopus 로고
    • Phages will out: Strategies of host cell lysis
    • Young, R., I. N. Wang, and W. D. Roof. 2000. Phages will out: strategies of host cell lysis. Trends Microbiol. 8:120-128.
    • (2000) Trends Microbiol , vol.8 , pp. 120-128
    • Young, R.1    Wang, I.N.2    Roof, W.D.3
  • 40
    • 0025019776 scopus 로고
    • Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli
    • Zagotta, M. T., and D. B. Wilson. 1990. Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli. J. Bacteriol. 172:912-921.
    • (1990) J. Bacteriol , vol.172 , pp. 912-921
    • Zagotta, M.T.1    Wilson, D.B.2


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