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Volumn 334, Issue 1, 2003, Pages 37-52

Defining the bacteriophage T4 DNA packaging machine: Evidence for a C-terminal DNA cleavage domain in the large terminase/packaging protein gp17

Author keywords

Combinatorial mutagenesis; DNA packaging; Nuclease active site; Phage T4; Terminase

Indexed keywords

CYSTEINE; HISTIDINE; NUCLEASE; PROTEIN; PROTEIN GP17; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 0142226893     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.028     Document Type: Article
Times cited : (37)

References (42)
  • 1
    • 0000154008 scopus 로고
    • Chromosome structure in phage T4. III. Terminal redundancy and length determination
    • Streisinger G., Emrich J., Stahl M.M. Chromosome structure in phage T4. III. Terminal redundancy and length determination. Proc. Natl Acad. Sci. USA. 57:1967;292-295.
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 292-295
    • Streisinger, G.1    Emrich, J.2    Stahl, M.M.3
  • 2
    • 0001026825 scopus 로고
    • DNA packaging in dsDNA bacteriophages
    • R. Calender. New York: Plenum Press
    • Black L.W. DNA packaging in dsDNA bacteriophages. Calender R. The Bacteriophages. The Bacteriophages. vol. 2:1988;321-373 Plenum Press, New York.
    • (1988) The Bacteriophages , vol.2 , pp. 321-373
    • Black, L.W.1
  • 3
    • 85030968086 scopus 로고    scopus 로고
    • Bacteriophage T4 DNA packaging
    • C. Catalano. Texas: Landes Biosciences. In press
    • Rao V., Black L.W. Bacteriophage T4 DNA packaging. Catalano C. Viral Genome Packaging. 2003;Landes Biosciences, Texas. In press.
    • (2003) Viral Genome Packaging
    • Rao, V.1    Black, L.W.2
  • 4
    • 0002036017 scopus 로고
    • Homologous recombination
    • J.D. Karam. Washington, DC: ASM Press
    • Mosig G. Homologous recombination. Karam J.D. Molecular Biology of Bacteriophage T4. 1994;54-82 ASM Press, Washington, DC.
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 54-82
    • Mosig, G.1
  • 5
    • 0002524555 scopus 로고
    • Nucleic acid packaging by viruses
    • S. Casjens. Boston: Jones and Bartlett
    • Casjens S. Nucleic acid packaging by viruses. Casjens S. Virus Structure and Assembly. 1985;76-147 Jones and Bartlett, Boston.
    • (1985) Virus Structure and Assembly , pp. 76-147
    • Casjens, S.1
  • 6
    • 0002067248 scopus 로고
    • Terminase and the recognition and cutting of chromosomes
    • Feiss M. Terminase and the recognition and cutting of chromosomes. Trends Genet. 2:1986;100-104.
    • (1986) Trends Genet. , vol.2 , pp. 100-104
    • Feiss, M.1
  • 8
    • 0023933829 scopus 로고
    • Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4: Construction of a defined in vitro packaging system using purified terminase proteins
    • Rao V.B., Black L.W. Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4: construction of a defined in vitro packaging system using purified terminase proteins. J. Mol. Biol. 200:1988;475-488.
    • (1988) J. Mol. Biol. , vol.200 , pp. 475-488
    • Rao, V.B.1    Black, L.W.2
  • 9
    • 0034711268 scopus 로고    scopus 로고
    • Biochemical characterization of an ATPase activity associated with the large packaging subunit gp17 from bacteriophage T4
    • Leffers G., Rao V.B. Biochemical characterization of an ATPase activity associated with the large packaging subunit gp17 from bacteriophage T4. J. Biol. Chem. 275:2000;37127-37136.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37127-37136
    • Leffers, G.1    Rao, V.B.2
  • 10
    • 0028916757 scopus 로고
    • Bacteriophage T4 gene 17 amplification mutants: Evidence for initiation by the T4 terminase subunit gp16
    • Wu C.H.H., Lin H., Black L.W. Bacteriophage T4 gene 17 amplification mutants: evidence for initiation by the T4 terminase subunit gp16. J. Mol. Biol. 247:1995;523-528.
    • (1995) J. Mol. Biol. , vol.247 , pp. 523-528
    • Wu, C.H.H.1    Lin, H.2    Black, L.W.3
  • 11
    • 0031023655 scopus 로고    scopus 로고
    • Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging
    • Lin H., Simon M.N., Black L.W. Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging. J. Biol. Chem. 272:1997;3495-3501.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3495-3501
    • Lin, H.1    Simon, M.N.2    Black, L.W.3
  • 12
    • 0033523081 scopus 로고    scopus 로고
    • Analysis of capsid portal protein and terminase functional domains: Interaction sites required for DNA packaging in bacteriophage T4
    • Lin H., Rao V.B., Black L.W. Analysis of capsid portal protein and terminase functional domains: interaction sites required for DNA packaging in bacteriophage T4. J. Mol. Biol. 289:1999;249-260.
    • (1999) J. Mol. Biol. , vol.289 , pp. 249-260
    • Lin, H.1    Rao, V.B.2    Black, L.W.3
  • 13
    • 0027217224 scopus 로고
    • A novel terminase activity associated with the DNA packaging proteins gp17 of bacteriophage T4
    • Bhattacharyya S.P., Rao V.B. A novel terminase activity associated with the DNA packaging proteins gp17 of bacteriophage T4. Virology. 196:1993;34-44.
    • (1993) Virology , vol.196 , pp. 34-44
    • Bhattacharyya, S.P.1    Rao, V.B.2
  • 14
    • 0038751848 scopus 로고    scopus 로고
    • Isolation and characterization of bacteriophage T4 gp17 terminase: A large subunit multimer with enhanced ATPase activity
    • Baumann R.G., Black L.W. Isolation and characterization of bacteriophage T4 gp17 terminase: a large subunit multimer with enhanced ATPase activity. J. Biol. Chem. 278:2003;4618-4623.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4618-4623
    • Baumann, R.G.1    Black, L.W.2
  • 15
    • 0032483313 scopus 로고    scopus 로고
    • Functional analysis of the DNA packaging/terminase protein gp17 from bacteriophage T4
    • Kuebler D., Rao V. Functional analysis of the DNA packaging/terminase protein gp17 from bacteriophage T4. J. Mol. Biol. 281:(5):1998;803-814.
    • (1998) J. Mol. Biol. , vol.281 , Issue.5 , pp. 803-814
    • Kuebler, D.1    Rao, V.2
  • 16
    • 0035976782 scopus 로고    scopus 로고
    • The N-terminal ATPase site in the large terminase protein gp17 is critically required for DNA packaging in bacteriophage T4
    • Rao V.B., Mitchell M.S. The N-terminal ATPase site in the large terminase protein gp17 is critically required for DNA packaging in bacteriophage T4. J. Mol. Biol. 314:2001;401-411.
    • (2001) J. Mol. Biol. , vol.314 , pp. 401-411
    • Rao, V.B.1    Mitchell, M.S.2
  • 17
    • 0037106323 scopus 로고    scopus 로고
    • Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases
    • Mitchell M.S., Matsuzaki S., Imai S., Rao V.B. Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucl. Acids Res. 30:2002;4009-4021.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 4009-4021
    • Mitchell, M.S.1    Matsuzaki, S.2    Imai, S.3    Rao, V.B.4
  • 18
    • 0026749374 scopus 로고
    • Mutations abolishing the endonuclease activity of bacteriophage lambda terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA-binding domain
    • Davidson A.R., Gold M. Mutations abolishing the endonuclease activity of bacteriophage lambda terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA-binding domain. Virology. 189:1992;21-30.
    • (1992) Virology , vol.189 , pp. 21-30
    • Davidson, A.R.1    Gold, M.2
  • 19
    • 0029129145 scopus 로고
    • Virus DNA packaging: The strategy used by phage lambda
    • Catalano C.E., Cue D., Feiss M. Virus DNA packaging: the strategy used by phage lambda. Mol. Microbiol. 16:1995;1075-1086.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 20
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3 dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi-29
    • Guo P., Peterson C., Anderson D. Prohead and DNA-gp3 dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi-29. J. Mol. Biol. 197:1987;229-236.
    • (1987) J. Mol. Biol. , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 21
    • 0033056680 scopus 로고    scopus 로고
    • Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga toxin as a phage late-gene product
    • Plunkett G., Rose D., Durfee T., Blattner F. Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga toxin as a phage late-gene product. J. Bacteriol. 181:1999;1767-1778.
    • (1999) J. Bacteriol. , vol.181 , pp. 1767-1778
    • Plunkett, G.1    Rose, D.2    Durfee, T.3    Blattner, F.4
  • 22
    • 26344480147 scopus 로고
    • Mechanistic principles of enzyme-catalyzed cleavage of phosphodiester bonds
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Glert J.A. Mechanistic principles of enzyme-catalyzed cleavage of phosphodiester bonds. Nucleases. 2nd edit. 1993;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) Nucleases 2nd edit.
    • Glert, J.A.1
  • 23
    • 0027289198 scopus 로고
    • The design of metal-binding sites in proteins
    • Regan L. The design of metal-binding sites in proteins. Annu. Rev. Biophys. Biomol. Struct. 22:1993;257-281.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 257-281
    • Regan, L.1
  • 24
    • 0025304132 scopus 로고
    • Genetic studies of the lac repressor. XIII. Extensive amino acid replacements generated by the use of natural and synthetic nonsense suppressors
    • Kleina L.G., Miller J. Genetic studies of the lac repressor. XIII. Extensive amino acid replacements generated by the use of natural and synthetic nonsense suppressors. J. Mol. Biol. 212:1990;295-318.
    • (1990) J. Mol. Biol. , vol.212 , pp. 295-318
    • Kleina, L.G.1    Miller, J.2
  • 25
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton R.M., Hunt H., Ho S., Pullen J., Pease L. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene. 77:1989;61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.2    Ho, S.3    Pullen, J.4    Pease, L.5
  • 26
    • 0034602290 scopus 로고    scopus 로고
    • Escherichia coli soft metal ion translocating ATPases
    • Gatti D., Mitra B., Rosen B.P. Escherichia coli soft metal ion translocating ATPases. J. Biol. Chem. 275:2000;34009-34012.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34009-34012
    • Gatti, D.1    Mitra, B.2    Rosen, B.P.3
  • 27
    • 0032741021 scopus 로고    scopus 로고
    • Vibriophage KVP40 and coliphage T4 genomes share a homologous 7-kb region immediately upstream of the gene encoding the major capsid protein
    • Matsuzaki S., Kuroda M., Kimura S., Tanaka S. Vibriophage KVP40 and coliphage T4 genomes share a homologous 7-kb region immediately upstream of the gene encoding the major capsid protein. Arch. Virol. 144:1999;2007-2012.
    • (1999) Arch. Virol. , vol.144 , pp. 2007-2012
    • Matsuzaki, S.1    Kuroda, M.2    Kimura, S.3    Tanaka, S.4
  • 29
    • 0038499685 scopus 로고    scopus 로고
    • Defining the ATPase center of bacteriophage T4 DNA packaging machine: Requirement for a catalytic glutamate in the large terminase protein gp17
    • Goetzinger K.R., Rao V.B. Defining the ATPase center of bacteriophage T4 DNA packaging machine: requirement for a catalytic glutamate in the large terminase protein gp17. J. Mol. Biol. 331:2003;139-154.
    • (2003) J. Mol. Biol. , vol.331 , pp. 139-154
    • Goetzinger, K.R.1    Rao, V.B.2
  • 30
    • 85030964870 scopus 로고    scopus 로고
    • Rentas, F. (2001). Molecular genetic and biochemical analysis of a putative terminase cutting site in the large DNA packaging protein gp17 from bacteriophage T4. PhD thesis, The Catholic University of America, Washington, DC.
    • Rentas, F. (2001). Molecular genetic and biochemical analysis of a putative terminase cutting site in the large DNA packaging protein gp17 from bacteriophage T4. PhD thesis, The Catholic University of America, Washington, DC.
  • 31
    • 0032030444 scopus 로고    scopus 로고
    • DNA requirements in vivo for phage T4 packaging
    • Lin H., Black L.W. DNA requirements in vivo for phage T4 packaging. Virology. 242:1998;118-127.
    • (1998) Virology , vol.242 , pp. 118-127
    • Lin, H.1    Black, L.W.2
  • 32
    • 0028040514 scopus 로고
    • Structural analysis of DNA cleaved in vivo by bacteriophage T4 terminase
    • Bhattacharyya S.P., Rao V.B. Structural analysis of DNA cleaved in vivo by bacteriophage T4 terminase. Gene. 146:1994;67-72.
    • (1994) Gene , vol.146 , pp. 67-72
    • Bhattacharyya, S.P.1    Rao, V.B.2
  • 33
    • 0032478529 scopus 로고    scopus 로고
    • The largest (70 kDa) product of the bacteriophage T4 DNA terminase gene 17 binds to single stranded DNA segments and digests them towards junctions with double-stranded DNA
    • Franklin J., Haseltine D., Davenport L., Mosig G. The largest (70 kDa) product of the bacteriophage T4 DNA terminase gene 17 binds to single stranded DNA segments and digests them towards junctions with double-stranded DNA. J. Mol. Biol. 277:1998;541-557.
    • (1998) J. Mol. Biol. , vol.277 , pp. 541-557
    • Franklin, J.1    Haseltine, D.2    Davenport, L.3    Mosig, G.4
  • 34
    • 0036303629 scopus 로고    scopus 로고
    • A bipartite bacteriophage T4 SOC and HOC randomized peptide display library: Detection and analysis of phage T4 terminase (gp17) and late σ factor (gp55) interaction
    • Malys N., Chang D.-Y., Baumann R.G., Xie D., Black L.W. A bipartite bacteriophage T4 SOC and HOC randomized peptide display library: detection and analysis of phage T4 terminase (gp17) and late σ factor (gp55) interaction. J. Mol. Biol. 319:2002;289-304.
    • (2002) J. Mol. Biol. , vol.319 , pp. 289-304
    • Malys, N.1    Chang, D.-Y.2    Baumann, R.G.3    Xie, D.4    Black, L.W.5
  • 35
    • 0022695021 scopus 로고
    • Potential metal-binding domains in nucleic acid binding proteins
    • Berg J.M. Potential metal-binding domains in nucleic acid binding proteins. Science. 232:1986;485-487.
    • (1986) Science , vol.232 , pp. 485-487
    • Berg, J.M.1
  • 36
    • 0027983134 scopus 로고
    • Analysis of functional domains of the packaging proteins of bacteriophage T3 by site-directed mutagenesis
    • Morita M., Tasaka M., Fujisawa H. Analysis of functional domains of the packaging proteins of bacteriophage T3 by site-directed mutagenesis. J. Mol. Biol. 235:1994;248-259.
    • (1994) J. Mol. Biol. , vol.235 , pp. 248-259
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 37
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang W., Steitz T.A. Recombining the structures of HIV integrase, RuvC and RNase H. Structure. 3:1995;131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 38
    • 0002598414 scopus 로고
    • Type II restriction endonucleases
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Roberts R.J., Halford S.E. Type II restriction endonucleases. Nucleases. 2nd edit. 1993;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) Nucleases 2nd edit.
    • Roberts, R.J.1    Halford, S.E.2
  • 39
    • 0028932881 scopus 로고
    • Structure and function of restriction endonucleases
    • Aggarwal A.K. Structure and function of restriction endonucleases. Curr. Opin. Struct. Biol. 5:1995;11-19.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 11-19
    • Aggarwal, A.K.1
  • 40
    • 0034634309 scopus 로고    scopus 로고
    • Endonuclease and helicase activities of bacteriophage lambda terminase: Changing nearby residue 515 restores activity to the gpA K497D mutant enzyme
    • Hwang Y., Hang J.Q., Neagle J., Duffy C., Feiss M. Endonuclease and helicase activities of bacteriophage lambda terminase: changing nearby residue 515 restores activity to the gpA K497D mutant enzyme. Virology. 277:2000;204-214.
    • (2000) Virology , vol.277 , pp. 204-214
    • Hwang, Y.1    Hang, J.Q.2    Neagle, J.3    Duffy, C.4    Feiss, M.5
  • 41
    • 0034730389 scopus 로고    scopus 로고
    • ATPase center of bacteriophage lambda terminase involved in post-cleavage stages of DNA packaging: Identification of ATP-interactive amino acids
    • Hang J.Q., Tack B., Feiss M. ATPase center of bacteriophage lambda terminase involved in post-cleavage stages of DNA packaging: identification of ATP-interactive amino acids. J. Mol. Biol. 302:2000;777-795.
    • (2000) J. Mol. Biol. , vol.302 , pp. 777-795
    • Hang, J.Q.1    Tack, B.2    Feiss, M.3
  • 42
    • 0028013205 scopus 로고
    • Direct sequencing of polymerase chain reaction-amplified DNA
    • Rao V.B. Direct sequencing of polymerase chain reaction-amplified DNA. Anal. Biochem. 216:1994;1-14.
    • (1994) Anal. Biochem. , vol.216 , pp. 1-14
    • Rao, V.B.1


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