메뉴 건너뛰기




Volumn 281, Issue 5, 1998, Pages 803-814

Functional analysis of the DNA-packaging/terminase protein gp17 from bacteriophage T4

Author keywords

ATP binding site; Bacteriophage T4; DNA packaging; Metal binding site; Terminase

Indexed keywords

BACTERIOPHAGE DNA; DOUBLE STRANDED DNA; HISTIDINE; VIRUS PROTEIN;

EID: 0032483313     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1952     Document Type: Article
Times cited : (40)

References (53)
  • 1
    • 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
  • 2
    • 0027217224 scopus 로고
    • A novel terminase activity associated with the DNA-packaging protein gp17 of bacteriophage T4
    • Bhattacharyya S.P., Rao V.B. A novel terminase activity associated with the DNA-packaging protein gp17 of bacteriophage T4. Virology. 196:1993;34-44
    • (1993) Virology , vol.196 , pp. 34-44
    • Bhattacharyya, S.P.1    Rao, V.B.2
  • 3
    • 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
  • 4
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H.C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl. Acids Res. 7:1979;1513-1523
    • (1979) Nucl. Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 5
    • 0001026825 scopus 로고
    • DNA Packaging in dsDNA Bacteriophages
    • Calender R. New York and London: Plenum Press
    • Black L.W. DNA Packaging in dsDNA Bacteriophages. Calender R. The Bacteriophages. 1988;321-374 Plenum Press, New York and London
    • (1988) The Bacteriophages , pp. 321-374
    • Black, L.W.1
  • 6
    • 0029556888 scopus 로고
    • DNA-packaging and cutting by phage terminases: Control in phage T4 by a synaptic mechanism
    • 1030
    • Black L.W. DNA-packaging and cutting by phage terminases control in phage T4 by a synaptic mechanism. Bioessays. 17:1995;1052. 1030
    • (1995) Bioessays , vol.17 , pp. 1052
    • Black, L.W.1
  • 7
    • 0025969881 scopus 로고
    • Suggestions for "safe" residue substitutions in site-directed mutagenesis
    • Bordo D., Argos P. Suggestions for "safe" residue substitutions in site-directed mutagenesis. J. Mol. Biol. 217:1991;721-729
    • (1991) J. Mol. Biol. , vol.217 , pp. 721-729
    • Bordo, D.1    Argos, P.2
  • 8
    • 0002524555 scopus 로고
    • Nucleic acid packaging by viruses
    • Casjens S. 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
  • 9
    • 0029129145 scopus 로고
    • Virus DNA-packaging: The strategy used by phage λ
    • Catalano C.E., Cue D., Feiss M. Virus DNA-packaging the strategy used by phage λ Mol. Microbiol. 16:1995;1075-1086
    • (1995) Mol. Microbiol. , vol.16 , pp. 1075-1086
    • Catalano, C.E.1    Cue, D.2    Feiss, M.3
  • 10
    • 0028089888 scopus 로고
    • An efficient site-directed mutagenesis method based on PCR
    • Chen B., Przybyla A.E. An efficient site-directed mutagenesis method based on PCR. Biotechniques. 17:1994;657-659
    • (1994) Biotechniques , vol.17 , pp. 657-659
    • Chen, B.1    Przybyla, A.E.2
  • 11
    • 0028818241 scopus 로고
    • Metal search: A computer program that helps design tetrahedral metal-binding sites
    • Clarke N.D., Yuan S.-M. Metal search a computer program that helps design tetrahedral metal-binding sites. Proteins: Struct. Funct. Genet. 23:1995;256-263
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 256-263
    • Clarke, N.D.1    Yuan, S.-M.2
  • 12
    • 0026749374 scopus 로고
    • Mutations abolishing the endonuclease activity of bacteriophage λ terminase lie in two distinct regions of theA gene, one of which may encode a leucine zipper DNA-binding domain
    • Davidson A.R., Gold M. Mutations abolishing the endonuclease activity of bacteriophage λ terminase lie in two distinct regions of theA 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
  • 13
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower W.J., Miller J.F., Ragsdale C.W. High efficiency transformation of E. coli by high voltage electroporation. Nucl. Acids Res. 16:1988;6127-6145
    • (1988) Nucl. Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 14
    • 0018932980 scopus 로고
    • DNA-packaging in dsDNA bacteriophages
    • Earnshaw W., Casjens S. DNA-packaging in dsDNA bacteriophages. Cell. 21:1980;319-331
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.1    Casjens, S.2
  • 15
    • 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
  • 16
    • 0022429775 scopus 로고
    • Processive action of terminase during sequential packaging of bacteriophage λ chromosomes
    • Feiss M., Sippy J., Miller G. Processive action of terminase during sequential packaging of bacteriophage λ chromosomes. J. Mol. Biol. 186:1985;759-771
    • (1985) J. Mol. Biol. , vol.186 , pp. 759-771
    • Feiss, M.1    Sippy, J.2    Miller, G.3
  • 17
    • 0021633925 scopus 로고
    • A functional domain of bacteriophage λ terminase for prohead binding
    • Frackman S., Siegele D.A., Feiss M. A functional domain of bacteriophage λ terminase for prohead binding. J. Mol. Biol. 180:1984;283-300
    • (1984) J. Mol. Biol. , vol.180 , pp. 283-300
    • Frackman, S.1    Siegele, D.A.2    Feiss, M.3
  • 18
    • 0021633925 scopus 로고
    • The terminase of bacteriophage λ: FFunctional domains for cos B binding and multimer assembly
    • Frackman S., Siegele D.A., Feiss M. The terminase of bacteriophage λ functional domains for cos B binding and multimer assembly. J. Mol. Biol. 180:1985;283-300
    • (1985) J. Mol. Biol. , vol.180 , pp. 283-300
    • Frackman, S.1    Siegele, D.A.2    Feiss, M.3
  • 19
    • 0030600476 scopus 로고    scopus 로고
    • Expression of the bacteriophage T4 DNA terminase genes 16 and 17 yields multiple proteins
    • Franklin J., Mosig G. Expression of the bacteriophage T4 DNA terminase genes 16 and 17 yields multiple proteins. Gene. 177:1996;179-189
    • (1996) Gene , vol.177 , pp. 179-189
    • Franklin, J.1    Mosig, G.2
  • 20
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by lon mutants of E. coli K12
    • Gottesman S., Halpern E., Trisler P. Role of sulA and sulB in filamentation by lon mutants of E. coli K12. J. Bacteriol. 148:1981;265-273
    • (1981) J. Bacteriol. , vol.148 , pp. 265-273
    • Gottesman, S.1    Halpern, E.2    Trisler, P.3
  • 21
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA-packaging protein gp16 of bacteriophage f29
    • Guo P., Peterson C., Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA-packaging protein gp16 of bacteriophage f29. 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
  • 22
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R., Krummel B., Saiki R.K. A general method of in vitro preparation and specific mutagenesis of DNA fragments study of protein and DNA interactions. Nucl. Acids Res. 16:1988;7351-7366
    • (1988) Nucl. Acids Res. , vol.16 , pp. 7351-7366
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 23
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., Pease L.R. 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.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 24
    • 0030606851 scopus 로고    scopus 로고
    • Mutations affecting the high affinity ATPase center of gpA, the large subunit of bacteriophage λ terminase, inactivate the endonuclease activity of terminase
    • Hwang Y., Feiss M. Mutations affecting the high affinity ATPase center of gpA, the large subunit of bacteriophage λ terminase, inactivate the endonuclease activity of terminase. J. Mol. Biol. 261:1996;524-535
    • (1996) J. Mol. Biol. , vol.261 , pp. 524-535
    • Hwang, Y.1    Feiss, M.2
  • 25
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H., Nojima H., Okayama H. High efficiency transformation of Escherichia coli with plasmids. Gene. 96:1990;23-28
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 26
    • 0025331936 scopus 로고
    • Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency
    • Kleina L.G., Masson J.-M., Normanly J., Abelson J., Miller J.H. Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency. J. Mol. Biol. 213:1990;705-717
    • (1990) J. Mol. Biol. , vol.213 , pp. 705-717
    • Kleina, L.G.1    Masson, J.-M.2    Normanly, J.3    Abelson, J.4    Miller, J.H.5
  • 27
    • 0342526807 scopus 로고    scopus 로고
    • A discontinuous headful packaging model for packaging less than headful length DNA molecules by bacteriophage T4
    • Leffers G., Rao V.B. A discontinuous headful packaging model for packaging less than headful length DNA molecules by bacteriophage T4. J. Mol. Biol. 258:1996;839-850
    • (1996) J. Mol. Biol. , vol.258 , pp. 839-850
    • Leffers, G.1    Rao, V.B.2
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0025788241 scopus 로고
    • High-fidelity amplification using a thermostable DNA polymersae isolated from Pyrococcus furiosus
    • Lundberg K.S., Shoemaker D.D., Adams M.W.W., Short J.M., Sorge J.A., Mathur E.J. High-fidelity amplification using a thermostable DNA polymersae isolated from Pyrococcus furiosus. Gene. 108:1991;1-6
    • (1991) Gene , vol.108 , pp. 1-6
    • Lundberg, K.S.1    Shoemaker, D.D.2    Adams, M.W.W.3    Short, J.M.4    Sorge, J.A.5    Mathur, E.J.6
  • 32
    • 0017409415 scopus 로고
    • Genetic identification of cloned fragments of bacteriophage T4 DNA and complementation by some clones containing early T4 genes
    • Mattson T., van Houwe G., Bolle A., Selzer G., Epstein R. Genetic identification of cloned fragments of bacteriophage T4 DNA and complementation by some clones containing early T4 genes. Mol. Gen. Genet. 154:1977;319-326
    • (1977) Mol. Gen. Genet. , vol.154 , pp. 319-326
    • Mattson, T.1    Van Houwe, G.2    Bolle, A.3    Selzer, G.4    Epstein, R.5
  • 33
    • 0028825192 scopus 로고
    • A simple and fast approach to prediction of protein secondary structure from multiply aligned sequences with accuracy above 70%
    • Mehta P.K., Heringa J., Argos P. A simple and fast approach to prediction of protein secondary structure from multiply aligned sequences with accuracy above 70%. J. Mol. Biol. 4:1995;2517-2525
    • (1995) J. Mol. Biol. , vol.4 , pp. 2517-2525
    • Mehta, P.K.1    Heringa, J.2    Argos, P.3
  • 34
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller J., McLachlan A.D., Klug A. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 4:1985;1609-1614
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 35
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki A., King J. Protein folding intermediates and inclusion body formation. Bio/Technology. 7:1989;690-697
    • (1989) Bio/Technology , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 36
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 37
    • 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
  • 38
    • 0028960132 scopus 로고
    • Structural and functional domains of the large subunit of the bacteriophage T3 DNA-packaging enzyme: Importance of the C-terminal region in prohead binding
    • Morita M., Tasaka M., Fujisawa H. Structural and functional domains of the large subunit of the bacteriophage T3 DNA-packaging enzyme importance of the C-terminal region in prohead binding. J. Mol. Biol. 245:1995;635-644
    • (1995) J. Mol. Biol. , vol.245 , pp. 635-644
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 39
    • 0024046830 scopus 로고
    • Lethal effect of λ terminase un recombination deficient E. coli
    • Murialdo H. Lethal effect of λ terminase un recombination deficient E. coli. Mol. Gen. Genet. 213:1988;42-49
    • (1988) Mol. Gen. Genet. , vol.213 , pp. 42-49
    • Murialdo, H.1
  • 41
    • 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
  • 42
    • 0023933829 scopus 로고
    • Cloning, overexpression, and purification of the terminase proteins gp16 and gp17 of bacteriophage T4: Construction of a defined in vitro DNA-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 DNA-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
  • 43
    • 13144271935 scopus 로고    scopus 로고
    • The small terminase subunit gp16 acts as an enhancer of DNA-packaging in bacteriophage T4
    • Asilomar, CA
    • Rao V.B., Leffers G. The small terminase subunit gp16 acts as an enhancer of DNA-packaging in bacteriophage T4. The 15th Biennial Conference on Phage/Virus Assembly. 1997;2.4. Asilomar, CA
    • (1997) The 15th Biennial Conference on Phage/Virus Assembly , pp. 24
    • Rao, V.B.1    Leffers, G.2
  • 44
    • 0026526051 scopus 로고
    • A phage T4 in vitro packaging system for cloning long DNA molecules
    • Rao V.B., Thaker V., Black L.W. A phage T4 in vitro packaging system for cloning long DNA molecules. Gene. 113:1992;25-33
    • (1992) Gene , vol.113 , pp. 25-33
    • Rao, V.B.1    Thaker, V.2    Black, L.W.3
  • 45
    • 2142852547 scopus 로고    scopus 로고
    • Molecular genetic and biochemical analysis of the DNA-packaging and terminase functions of gp 17 from bacteriophage T4
    • Olympia, WA
    • Rao V.B., Leffers G., Kuebler D. Molecular genetic and biochemical analysis of the DNA-packaging and terminase functions of gp 17 from bacteriophage T4. The 11th Evergreen International Bacteriophage T4 Meeting. 1996;28. Olympia, WA
    • (1996) The 11th Evergreen International Bacteriophage T4 Meeting , pp. 28
    • Rao, V.B.1    Leffers, G.2    Kuebler, D.3
  • 46
    • 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
  • 47
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. Protein design novel metal-binding sites. Trends Biochem. Sci. 20:1995;280-284
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 280-284
    • Regan, L.1
  • 48
    • 0001668425 scopus 로고
    • The reaction of nitrous acid with deoxyribonucleic acid
    • Schuster H. The reaction of nitrous acid with deoxyribonucleic acid. Biophys. Biochem. Res. Commun. 2:1960;320-323
    • (1960) Biophys. Biochem. Res. Commun. , vol.2 , pp. 320-323
    • Schuster, H.1
  • 49
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story R.M., Steitz T.A. Structure of the recA protein-ADP complex. Nature. 355:1992;374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 50
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • Studier W., Rosenberg A.H., Dunn J.J. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:1990;61-89
    • (1990) Methods Enzymol. , vol.185 , pp. 61-89
    • Studier, W.1    Rosenberg, A.H.2    Dunn, J.J.3
  • 51
    • 0001607723 scopus 로고
    • Distinctly related sequences in the α- And β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Sarasate M., Runswick M.J., Gay N.J. Distinctly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Sarasate, M.2    Runswick, M.J.3    Gay, N.J.4
  • 52
    • 0028873717 scopus 로고
    • Mutational analysis of the prohead binding domain of the large subunit of terminase, the bacteriophage λ DNA-packaging enzyme
    • Yeo A., Feiss M. Mutational analysis of the prohead binding domain of the large subunit of terminase, the bacteriophage λ DNA-packaging enzyme. J. Mol. Biol. 245:1995;126-140
    • (1995) J. Mol. Biol. , vol.245 , pp. 126-140
    • Yeo, A.1    Feiss, M.2
  • 53
    • 0030575801 scopus 로고    scopus 로고
    • Novel mutants in the 5′-upstream region of the portal protein gene 20 overcome a gp40-dependent prohead assembly block in bacteriophage T4
    • Yap N.L., Rao V.B. Novel mutants in the 5′-upstream region of the portal protein gene 20 overcome a gp40-dependent prohead assembly block in bacteriophage T4. J. Mol. Biol. 263:1996;539-550
    • (1996) J. Mol. Biol. , vol.263 , pp. 539-550
    • Yap, N.L.1    Rao, V.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.