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Volumn 89, Issue 4, 2013, Pages 702-714

Role of antifeeding prophage (Afp) protein Afp16 in terminating the length of the Afp tailocin and stabilizing its sheath

Author keywords

[No Author keywords available]

Indexed keywords

AFP16 PROTEIN; BACTERIAL PROTEIN; TAILOCIN; TUBE BASEPLATE COMPLEX; UNCLASSIFIED DRUG;

EID: 84881529117     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12305     Document Type: Article
Times cited : (28)

References (44)
  • 1
    • 0003535936 scopus 로고
    • Agresti, A. (ed.) New York: John Wiley & Sons.
    • Agresti, A. (ed.) (1990) Categorical Data Analysis. New York: John Wiley & Sons.
    • (1990) Categorical Data Analysis
  • 3
    • 0030065304 scopus 로고    scopus 로고
    • Gut pH and amylase and protease activity in larvae of the New Zealand grass grub (Costelytra zealandica; Coleoptera: Scarabaeidae) as a basis for selecting inhibitors
    • Biggs, D.R., and McGregor, P.G. (1996) Gut pH and amylase and protease activity in larvae of the New Zealand grass grub (Costelytra zealandica; Coleoptera: Scarabaeidae) as a basis for selecting inhibitors. Insect Biochem Mol Biol 26: 69-75.
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 69-75
    • Biggs, D.R.1    McGregor, P.G.2
  • 4
    • 0015097555 scopus 로고
    • Self-assembly of bacteriophage lambda tails
    • Bleviss, M., and Easterbrook, K.B. (1971) Self-assembly of bacteriophage lambda tails. Can J Microbiol 17: 947-954.
    • (1971) Can J Microbiol , vol.17 , pp. 947-954
    • Bleviss, M.1    Easterbrook, K.B.2
  • 5
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H.J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8: 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 6
    • 77952139886 scopus 로고    scopus 로고
    • Tubules and donuts: a type VI secretion story
    • Bönemann, G., Pietrosiuk, A., and Mogk, A. (2010) Tubules and donuts: a type VI secretion story. Mol Microbiol 76: 815-821.
    • (2010) Mol Microbiol , vol.76 , pp. 815-821
    • Bönemann, G.1    Pietrosiuk, A.2    Mogk, A.3
  • 8
    • 33645854351 scopus 로고    scopus 로고
    • Length control of extended protein structures in bacteria and bacteriophages
    • Cornelis, G.R., Agrain, C., and Sorg, I. (2006) Length control of extended protein structures in bacteria and bacteriophages. Curr Opin Microbiol 9: 201-206.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 201-206
    • Cornelis, G.R.1    Agrain, C.2    Sorg, I.3
  • 9
    • 33751412840 scopus 로고    scopus 로고
    • The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function
    • Edmonds, L., Liu, A., Kwan, J.J., Avanessy, A., Caracoglia, M., Yang, I., etal. (2007) The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function. J Mol Biol 365: 175-186.
    • (2007) J Mol Biol , vol.365 , pp. 175-186
    • Edmonds, L.1    Liu, A.2    Kwan, J.J.3    Avanessy, A.4    Caracoglia, M.5    Yang, I.6
  • 11
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • Grossman, T.H., Kawasaki, E.S., Punreddy, S.R., and Osburne, M.S. (1998) Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209: 95-103.
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 12
    • 0021848276 scopus 로고
    • Morphogenetic structures present in lysates of amber mutants of bacteriophage Mu
    • Grundy, F.J., and Howe, M.M. (1985) Morphogenetic structures present in lysates of amber mutants of bacteriophage Mu. Virology 143: 485-504.
    • (1985) Virology , vol.143 , pp. 485-504
    • Grundy, F.J.1    Howe, M.M.2
  • 13
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Höfte, H., and Whiteley, H.R. (1989) Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol Mol Biol Rev 53: 242-255.
    • (1989) Microbiol Mol Biol Rev , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 14
    • 3242808947 scopus 로고    scopus 로고
    • Cloning Serratia entomophila antifeeding genes - a putative defective prophage active against the grass grub Costelytra zealandica
    • Hurst, M.R.H., Glare, T.R., and Jackson, T.A. (2004) Cloning Serratia entomophila antifeeding genes - a putative defective prophage active against the grass grub Costelytra zealandica. J Bacteriol 186: 5116-5128.
    • (2004) J Bacteriol , vol.186 , pp. 5116-5128
    • Hurst, M.R.H.1    Glare, T.R.2    Jackson, T.A.3
  • 15
    • 34247156738 scopus 로고    scopus 로고
    • Isolation and characterization of the Serratia entomophila antifeeding prophage
    • Hurst, M.R.H., Beard, S.S., Jackson, T.A., and Jones, S.M. (2007) Isolation and characterization of the Serratia entomophila antifeeding prophage. FEMS Microbiol Lett 270: 42-48.
    • (2007) FEMS Microbiol Lett , vol.270 , pp. 42-48
    • Hurst, M.R.H.1    Beard, S.S.2    Jackson, T.A.3    Jones, S.M.4
  • 16
    • 78650744470 scopus 로고    scopus 로고
    • Nucleotide sequence of the Serratia entomophila plasmid pADAP and the Serratia proteamaculans pU143 plasmid virulence associated region
    • Hurst, M.R.H., Becher, S.A., and O'Callaghan, M. (2011) Nucleotide sequence of the Serratia entomophila plasmid pADAP and the Serratia proteamaculans pU143 plasmid virulence associated region. Plasmid 65: 32-41.
    • (2011) Plasmid , vol.65 , pp. 32-41
    • Hurst, M.R.H.1    Becher, S.A.2    O'Callaghan, M.3
  • 17
    • 85010248486 scopus 로고
    • The fine structure of a pyocin
    • Ishii, S.-i., Nishi, Y., and Egami, F. (1965) The fine structure of a pyocin. J Mol Biol 13: 428-431.
    • (1965) J Mol Biol , vol.13 , pp. 428-431
    • Ishii, S.-i.1    Nishi, Y.2    Egami, F.3
  • 18
    • 0016372164 scopus 로고
    • A regulator protein for the length determination of bacteriophage lambda tail
    • Katsura, I., and Kühl, P.W. (1974) A regulator protein for the length determination of bacteriophage lambda tail. J Supramol Struct 2: 239-252.
    • (1974) J Supramol Struct , vol.2 , pp. 239-252
    • Katsura, I.1    Kühl, P.W.2
  • 19
    • 0017336648 scopus 로고
    • Purification and characterization of the major protein and the terminator protein of the bacteriophage λ tail
    • Katsura, I., and Tsugita, A. (1977) Purification and characterization of the major protein and the terminator protein of the bacteriophage λ tail. Virology 76: 129-145.
    • (1977) Virology , vol.76 , pp. 129-145
    • Katsura, I.1    Tsugita, A.2
  • 20
    • 0014355314 scopus 로고
    • Electron microscope studies of mutants of lambda bacteriophage: I. General description and quantitation of viral products
    • Kemp, C.L., Howatson, A.F., and Siminovitch, L. (1968) Electron microscope studies of mutants of lambda bacteriophage: I. General description and quantitation of viral products. Virology 36: 490-502.
    • (1968) Virology , vol.36 , pp. 490-502
    • Kemp, C.L.1    Howatson, A.F.2    Siminovitch, L.3
  • 21
    • 0016587670 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis: II. Mutants unable to form the central part of the baseplate
    • Kikuchi, Y., and King, J. (1975) Genetic control of bacteriophage T4 baseplate morphogenesis: II. Mutants unable to form the central part of the baseplate. J Mol Biol 99: 673-694.
    • (1975) J Mol Biol , vol.99 , pp. 673-694
    • Kikuchi, Y.1    King, J.2
  • 22
    • 0014413431 scopus 로고
    • Assembly of the tail of bacteriophage T4
    • King, J. (1968) Assembly of the tail of bacteriophage T4. J Mol Biol 32: 231-262.
    • (1968) J Mol Biol , vol.32 , pp. 231-262
    • King, J.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 61849164427 scopus 로고    scopus 로고
    • Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin
    • Leiman, P.G., Basler, M., Ramagopal, U.A., Bonanno, J.B., Sauder, J.M., Pukatzki, S., etal. (2009) Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proc Natl Acad Sci USA 106: 4154-4159.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4154-4159
    • Leiman, P.G.1    Basler, M.2    Ramagopal, U.A.3    Bonanno, J.B.4    Sauder, J.M.5    Pukatzki, S.6
  • 27
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S.J., Baldwin, P.R., and Chiu, W. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 28
    • 8444247520 scopus 로고    scopus 로고
    • Cellular length control systems
    • Marshall, W.F. (2004) Cellular length control systems. Annu Rev Cell Dev Biol 20: 677-693.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 677-693
    • Marshall, W.F.1
  • 29
    • 0014289388 scopus 로고
    • Mutations in bacteriophage lambda affecting particle morphogenesis
    • Mount, D.W.A., Harris, A.W., Fuerst, C.R., and Siminovitch, L. (1968) Mutations in bacteriophage lambda affecting particle morphogenesis. Virology 35: 134-149.
    • (1968) Virology , vol.35 , pp. 134-149
    • Mount, D.W.A.1    Harris, A.W.2    Fuerst, C.R.3    Siminovitch, L.4
  • 30
    • 0033744629 scopus 로고    scopus 로고
    • The R-type pyocin of Pseudomonas aeruginosa is related to P2 phage, and the F-type is related to lambda phage
    • Nakayama, K., Takashima, K., Ishihara, H., Shinomiya, T., Kageyama, M., Kanaya, S., etal. (2000) The R-type pyocin of Pseudomonas aeruginosa is related to P2 phage, and the F-type is related to lambda phage. Mol Microbiol 38: 213-231.
    • (2000) Mol Microbiol , vol.38 , pp. 213-231
    • Nakayama, K.1    Takashima, K.2    Ishihara, H.3    Shinomiya, T.4    Kageyama, M.5    Kanaya, S.6
  • 31
    • 61849155151 scopus 로고    scopus 로고
    • The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
    • Pell, L.G., Kanelis, V., Donaldson, L.W., Lynne Howell, P., and Davidson, A.R. (2009a) The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci USA 106: 4160-4165.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4160-4165
    • Pell, L.G.1    Kanelis, V.2    Donaldson, L.W.3    Lynne Howell, P.4    Davidson, A.R.5
  • 32
    • 67349236770 scopus 로고    scopus 로고
    • The X-Ray crystal structure of the phage λ tail terminator protein reveals the biologically relevant hexameric ring structure and demonstrates a conserved mechanism of tail termination among diverse long-tailed phages
    • Pell, L.G., Liu, A., Edmonds, L., Donaldson, L.W., Howell, P.L., and Davidson, A.R. (2009b) The X-Ray crystal structure of the phage λ tail terminator protein reveals the biologically relevant hexameric ring structure and demonstrates a conserved mechanism of tail termination among diverse long-tailed phages. J Mol Biol 389: 938-951.
    • (2009) J Mol Biol , vol.389 , pp. 938-951
    • Pell, L.G.1    Liu, A.2    Edmonds, L.3    Donaldson, L.W.4    Howell, P.L.5    Davidson, A.R.6
  • 33
    • 79251523486 scopus 로고    scopus 로고
    • The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus' encodes an afp-like prophage possibly used for protein secretion
    • Penz, T., Horn, M., and Schmitz-Esser, S. (2010) The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus' encodes an afp-like prophage possibly used for protein secretion. Virulence 1: 541-545.
    • (2010) Virulence , vol.1 , pp. 541-545
    • Penz, T.1    Horn, M.2    Schmitz-Esser, S.3
  • 34
    • 84868089864 scopus 로고    scopus 로고
    • Comparative genomics suggests an independent origin of cytoplasmic incompatibility in Cardinium hertigii
    • Penz, T., Schmitz-Esser, S., Kelly, S.E., Cass, B.N., Müller, A., Woyke, T., etal. (2012) Comparative genomics suggests an independent origin of cytoplasmic incompatibility in Cardinium hertigii. PLoS Genet 8: e1003012.
    • (2012) PLoS Genet , vol.8
    • Penz, T.1    Schmitz-Esser, S.2    Kelly, S.E.3    Cass, B.N.4    Müller, A.5    Woyke, T.6
  • 36
    • 0003903343 scopus 로고
    • Sambrook, J., Fritsch, E.F., Maniatis, T., and Laboratory, C.S.H. (eds), New York: Cold Spring Harbor Laboratory Press.
    • Sambrook, J., Fritsch, E.F., Maniatis, T., and Laboratory, C.S.H. (eds) (1989) Molecular Cloning: A Laboratory Manual. New York: Cold Spring Harbor Laboratory Press.
    • (1989) Molecular Cloning: A Laboratory Manual
  • 37
    • 77956511889 scopus 로고    scopus 로고
    • Structural study of the Serratia entomophila antifeeding prophage: three-dimensional structure of the helical sheath
    • Sen, A., Rybakova, D., Hurst, M.R.H., and Mitra, A.K. (2010) Structural study of the Serratia entomophila antifeeding prophage: three-dimensional structure of the helical sheath. J Bacteriol 192: 4522-4525.
    • (2010) J Bacteriol , vol.192 , pp. 4522-4525
    • Sen, A.1    Rybakova, D.2    Hurst, M.R.H.3    Mitra, A.K.4
  • 38
    • 0014694376 scopus 로고
    • Disassembly of T-even bacteriophage into structural parts and subunits
    • To, C.M., Kellenberger, E., and Eisenstark, A. (1969) Disassembly of T-even bacteriophage into structural parts and subunits. J Mol Biol 46: 493-511.
    • (1969) J Mol Biol , vol.46 , pp. 493-511
    • To, C.M.1    Kellenberger, E.2    Eisenstark, A.3
  • 39
    • 0020418108 scopus 로고
    • Incidence and transmission of a disease of grass grub (Costelytra zealandica) in Canterbury
    • Trought, T.E.T., Jackson, T.A., and French, R.A. (1982) Incidence and transmission of a disease of grass grub (Costelytra zealandica) in Canterbury. N Z J Exp Agr 10: 79-82.
    • (1982) N Z J Exp Agr , vol.10 , pp. 79-82
    • Trought, T.E.T.1    Jackson, T.A.2    French, R.A.3
  • 40
    • 0033983898 scopus 로고    scopus 로고
    • Bacteriophage T4 self-assembly: localization of gp3 and its role in determining tail length
    • Vianelli, A., Wang, G.R., Gingery, M., Duda, R.L., Eiserling, F.A., and Goldberg, E.B. (2000) Bacteriophage T4 self-assembly: localization of gp3 and its role in determining tail length. J Bacteriol 182: 680-688.
    • (2000) J Bacteriol , vol.182 , pp. 680-688
    • Vianelli, A.1    Wang, G.R.2    Gingery, M.3    Duda, R.L.4    Eiserling, F.A.5    Goldberg, E.B.6
  • 41
    • 3943110336 scopus 로고    scopus 로고
    • Insect pathogenicity islands in the insect pathogenic bacterium Photorhabdus
    • Waterfield, N.R., Daborn, P.J., and ffrench-Constant, R.H. (2004) Insect pathogenicity islands in the insect pathogenic bacterium Photorhabdus. Physiol Entomol 29: 240-250.
    • (2004) Physiol Entomol , vol.29 , pp. 240-250
    • Waterfield, N.R.1    Daborn, P.J.2    ffrench-Constant, R.H.3
  • 42
    • 33644865190 scopus 로고    scopus 로고
    • Photorhabdus virulence cassettes confer injectable insecticidal activity against the wax moth
    • Yang, G., Dowling, A.J., Gerike, U., ffrench-Constant, R.H., and Waterfield, N.R. (2006) Photorhabdus virulence cassettes confer injectable insecticidal activity against the wax moth. J Bacteriol 188: 2254-2261.
    • (2006) J Bacteriol , vol.188 , pp. 2254-2261
    • Yang, G.1    Dowling, A.J.2    Gerike, U.3    ffrench-Constant, R.H.4    Waterfield, N.R.5
  • 43
    • 84862602464 scopus 로고    scopus 로고
    • Polymorphic toxin systems: comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics
    • Zhang, D., de Souza, R.F., Anantharaman, V., Lyer, L.M., and Aravind, L. (2012) Polymorphic toxin systems: comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics. Biol Direct 7: 18.
    • (2012) Biol Direct , vol.7 , pp. 18
    • Zhang, D.1    de Souza, R.F.2    Anantharaman, V.3    Lyer, L.M.4    Aravind, L.5
  • 44
    • 0037369791 scopus 로고    scopus 로고
    • P15 and P3, the tail completion proteins of bacteriophage T4, both form hexameric rings
    • Zhao, L., Kanamaru, S., Chaidirek, C.C., and Arisaka, F. (2003) P15 and P3, the tail completion proteins of bacteriophage T4, both form hexameric rings. J Bacteriol 185: 1693-1700.
    • (2003) J Bacteriol , vol.185 , pp. 1693-1700
    • Zhao, L.1    Kanamaru, S.2    Chaidirek, C.C.3    Arisaka, F.4


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