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Volumn 265, Issue 2, 1999, Pages 196-205

A mutation correcting the DNA interaction defects of a mutant phage λ terminase, gpNu1 K35A terminase

Author keywords

Genome encapsidation; Virus assembly; Virus genome packaging

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; HELIX LOOP HELIX PROTEIN;

EID: 0033590162     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.0055     Document Type: Article
Times cited : (3)

References (56)
  • 1
    • 0001944551 scopus 로고
    • Experimental methods for use with lambda
    • (R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg, Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Arber, W., Enquist, L., Hohn, B., Murray, N. E., and Murray, K.1983. Experimental methods for use with lambda. InLambda II (R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg, Eds.), pp. 433-466. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1983) InLambda II , pp. 433-466
    • Arber, W.1    Enquist, L.2    Hohn, B.3    Murray, N.E.4    Murray, K.5
  • 2
    • 0032146388 scopus 로고    scopus 로고
    • ATP-reactive sites in the bacteriophage λ packaging protein terminase lie in the N-termini of its subunits, gpA and gpNu1
    • Babbar B. K., Gold M. ATP-reactive sites in the bacteriophage λ packaging protein terminase lie in the N-termini of its subunits, gpA and gpNu1. Virology. 247:1998;251-264.
    • (1998) Virology , vol.247 , pp. 251-264
    • Babbar, B.K.1    Gold, M.2
  • 3
    • 0024278077 scopus 로고
    • Prediction of an ATP reactive center in the small subunit, gpNu1, of the phage lambda terminase enzyme
    • Becker A., Gold M. Prediction of an ATP reactive center in the small subunit, gpNu1, of the phage lambda terminase enzyme. J. Mol. Biol. 199:1988;219-222.
    • (1988) J. Mol. Biol. , vol.199 , pp. 219-222
    • Becker, A.1    Gold, M.2
  • 4
    • 0025362781 scopus 로고
    • Bacteriophage lambda DNA: The beginning of the end
    • Becker A., Murialdo H. Bacteriophage lambda DNA: The beginning of the end. J. Bacteriol. 172:1990;2819-2824.
    • (1990) J. Bacteriol. , vol.172 , pp. 2819-2824
    • Becker, A.1    Murialdo, H.2
  • 5
    • 0017737569 scopus 로고
    • Early events in the in vitro packaging of bacteriophage DNA
    • Becker A., Murialdo H., Gold M. Early events in the in vitro packaging of bacteriophage DNA. Virology. 78:1977;291-305.
    • (1977) Virology , vol.78 , pp. 291-305
    • Becker, A.1    Murialdo, H.2    Gold, M.3
  • 6
    • 0023898550 scopus 로고
    • Bacteriophage lambda DNA packaging. The product of the FI gene promotes the incorporation of the prohead to the DNA-terminase complex
    • Becker A., Murialdo H., Lucko H., Morell J. Bacteriophage lambda DNA packaging. The product of the FI gene promotes the incorporation of the prohead to the DNA-terminase complex. J. Mol. Biol. 199:1988;597-607.
    • (1988) J. Mol. Biol. , vol.199 , pp. 597-607
    • Becker, A.1    Murialdo, H.2    Lucko, H.3    Morell, J.4
  • 7
    • 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. Nucleic Acids Res. 7:1979;1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 8
    • 0015243879 scopus 로고
    • The arrangement of DNA in lambda phage heads. I Biological consequences of micrococcal nuclease attack on a portion of the chromosome exposed in tailless heads
    • Bode V. C., Gillin F. D. The arrangement of DNA in lambda phage heads. I Biological consequences of micrococcal nuclease attack on a portion of the chromosome exposed in tailless heads. J. Mol. Biol. 62:1971;493-502.
    • (1971) J. Mol. Biol. , vol.62 , pp. 493-502
    • Bode, V.C.1    Gillin, F.D.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 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
  • 11
    • 0028884710 scopus 로고
    • Inactivation of DNA polymerase alpha-primase by acrolein: Loss of activity depends on the DNA substrate
    • Catalano C. E., Kuchta R. D. Inactivation of DNA polymerase alpha-primase by acrolein: Loss of activity depends on the DNA substrate. Biochem. Biophys. Res. Commun. 214:1995;971-977.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 971-977
    • Catalano, C.E.1    Kuchta, R.D.2
  • 12
    • 0023541609 scopus 로고
    • The overproduction of DNA terminase of coliphage lambda
    • Chow S., Daub E., Murialdo H. The overproduction of DNA terminase of coliphage lambda. Gene. 60:1987;277-289.
    • (1987) Gene , vol.60 , pp. 277-289
    • Chow, S.1    Daub, E.2    Murialdo, H.3
  • 13
    • 0027146278 scopus 로고
    • The role of cosB, the binding site for terminase, the DNA packaging enzyme of bacteriophage lambda, in the nicking reaction
    • Cue D., Feiss M. The role of cosB, the binding site for terminase, the DNA packaging enzyme of bacteriophage lambda, in the nicking reaction. J. Mol. Biol. 234:1993a;594-609.
    • (1993) J. Mol. Biol. , vol.234 , pp. 594-609
    • Cue, D.1    Feiss, M.2
  • 14
    • 0027423324 scopus 로고
    • A site required for termination of packaging of the phage lambda chromosome
    • Cue D., Feiss M. A site required for termination of packaging of the phage lambda chromosome. Proc. Natl. Acad. Sci. USA. 90:1993b;9290-9294.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9290-9294
    • Cue, D.1    Feiss, M.2
  • 15
    • 0030884808 scopus 로고    scopus 로고
    • Genetic evidence that recognition of cosQ, the signal for termination of phage λ DNA packaging, depends on the extent of head filling
    • Cue D., Feiss M. Genetic evidence that recognition of cosQ, the signal for termination of phage λ DNA packaging, depends on the extent of head filling. Genetics. 147:1997;7-17.
    • (1997) Genetics , vol.147 , pp. 7-17
    • Cue, D.1    Feiss, M.2
  • 16
    • 0001035136 scopus 로고
    • Completed annotated lambda sequence
    • (J. Roberts, F. Stahl, and R. Weisberg, Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Daniels, D., Schroeder, J., Szybalski, W., Sanger, F., Coulsen, A., Hong, D., Hill, D., Peterson, G., and Blattner, F.1983. Completed annotated lambda sequence. InLambda II (J. Roberts, F. Stahl, and R. Weisberg, Eds.), pp. 519-676. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1983) InLambda II , pp. 519-676
    • Daniels, D.1    Schroeder, J.2    Szybalski, W.3    Sanger, F.4    Coulsen, A.5    Hong, D.6    Hill, D.7    Peterson, G.8    Blattner, F.9
  • 17
    • 0023474746 scopus 로고
    • A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage λ FI gene product
    • Davidson A., Gold M. A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage λ FI gene product. Virology. 161:1987;305-315.
    • (1987) Virology , vol.161 , pp. 305-315
    • Davidson, A.1    Gold, M.2
  • 18
    • 0000000628 scopus 로고
    • Mutations abolishing the endonuclease activity of bacteriophage λ terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA binding domain
    • Davidson A., Gold M. Mutations abolishing the endonuclease activity of bacteriophage λ terminase lie in two distinct regions of the A gene, one of which may encode a leucine zipper DNA binding domain. Virology. 161:1992;305-315.
    • (1992) Virology , vol.161 , pp. 305-315
    • Davidson, A.1    Gold, M.2
  • 19
    • 0018932980 scopus 로고
    • DNA packaging by the double-stranded DNA bacteriophages
    • Earnshaw W. C., Casjens S. R. DNA packaging by the double-stranded DNA bacteriophages. Cell. 21:1980;319-331.
    • (1980) Cell , vol.21 , pp. 319-331
    • Earnshaw, W.C.1    Casjens, S.R.2
  • 20
    • 0002067248 scopus 로고
    • Terminase and the recognition, cutting and packaging of λ chromosomes
    • Feiss M. Terminase and the recognition, cutting and packaging of λ chromosomes. Trends Genet. 2:1986;100-104.
    • (1986) Trends Genet. , vol.2 , pp. 100-104
    • Feiss, M.1
  • 21
    • 0020501606 scopus 로고
    • Structure of the bacteriophage lambda cohesive end site: Location of the sites of terminase binding (cosB) and nicking (cosN)
    • Feiss M., Widner W., Miller G., Johnson G., Christiansen S. Structure of the bacteriophage lambda cohesive end site: Location of the sites of terminase binding (cosB) and nicking (cosN). Gene. 24:1983;207-218.
    • (1983) Gene , vol.24 , pp. 207-218
    • Feiss, M.1    Widner, W.2    Miller, G.3    Johnson, G.4    Christiansen, S.5
  • 22
    • 0016292997 scopus 로고
    • Mutational specificity of a conditional Escherichia coli mutator, mutD5
    • Fowler R. G., Degner G. E., Cox E. C. Mutational specificity of a conditional Escherichia coli mutator, mutD5. Mol. Gen. Genet. 133:1974;179-191.
    • (1974) Mol. Gen. Genet. , vol.133 , pp. 179-191
    • Fowler, R.G.1    Degner, G.E.2    Cox, E.C.3
  • 23
    • 0022432143 scopus 로고
    • The terminase of bacteriophage lambda. Functional domains for cosB binding and multimer assembly
    • Frackman S., Siegele D. A., Feiss M. The terminase of bacteriophage lambda. Functional domains for cosB binding and multimer assembly. J. Mol. Biol. 183:1985;225-238.
    • (1985) J. Mol. Biol. , vol.183 , pp. 225-238
    • Frackman, S.1    Siegele, D.A.2    Feiss, M.3
  • 24
    • 0021100395 scopus 로고
    • The bacteriophage λ terminase: Partial purification and preliminary characterization of properties
    • Gold M., Becker A. The bacteriophage λ terminase: Partial purification and preliminary characterization of properties. J. Biol. Chem. 258:1983;14619-14625.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14619-14625
    • Gold, M.1    Becker, A.2
  • 25
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29
    • Guo P., Peterson C., Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ29. 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
  • 26
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:1983;557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 27
    • 0028560406 scopus 로고
    • Chromosome end formation in phage lambda, catalyzed by terminase, is controlled by two DNA elements of cos, cosN and R3, and by ATP
    • Higgins R. R., Becker A. Chromosome end formation in phage lambda, catalyzed by terminase, is controlled by two DNA elements of cos, cosN and R3, and by ATP. EMBO J. 13:1994a;6152-6161.
    • (1994) EMBO J. , vol.13 , pp. 6152-6161
    • Higgins, R.R.1    Becker, A.2
  • 28
    • 0028568276 scopus 로고
    • The lambda terminase enzyme measures the point of its endonucleolytic attack 47 ± 2 bp away from its site of specific DNA binding, the R site
    • Higgins R. R., Becker A. The lambda terminase enzyme measures the point of its endonucleolytic attack 47 ± 2 bp away from its site of specific DNA binding, the R site. EMBO J. 13:1994b;6162-6171.
    • (1994) EMBO J. , vol.13 , pp. 6162-6171
    • Higgins, R.R.1    Becker, A.2
  • 29
    • 0023788430 scopus 로고
    • Mechanism of cos DNA cleavage by bacteriophage lambda terminase: Multiple roles of ATP
    • Higgins R. R., Lucko H. J., Becker A. Mechanism of cos DNA cleavage by bacteriophage lambda terminase: Multiple roles of ATP. Cell. 54:1988;765-775.
    • (1988) Cell , vol.54 , pp. 765-775
    • Higgins, R.R.1    Lucko, H.J.2    Becker, A.3
  • 30
    • 0029920552 scopus 로고    scopus 로고
    • Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage λ
    • Hwang Y., Catalano C. E., Feiss M. Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage λ Biochemistry. 35:1996;2796-2803.
    • (1996) Biochemistry , vol.35 , pp. 2796-2803
    • Hwang, Y.1    Catalano, C.E.2    Feiss, M.3
  • 31
    • 0029082986 scopus 로고
    • A defined system for in vitro lambda DNA packaging
    • Hwang Y., Feiss M. A defined system for in vitro lambda DNA packaging. Virology. 211:1995;367-376.
    • (1995) Virology , vol.211 , pp. 367-376
    • Hwang, Y.1    Feiss, M.2
  • 32
    • 0030606851 scopus 로고    scopus 로고
    • Mutations affecting the high affinity ATPase center of gpA, the large subunit of bacteriophage lambda 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 lambda 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
  • 33
    • 0030919259 scopus 로고    scopus 로고
    • Mutations affecting lysine-35 of gpNu1, the small subunit of bacteriophage λ terminase, alter the strength and specificity of holoterminase interactions with DNA
    • Hwang Y., Feiss M. Mutations affecting lysine-35 of gpNu1, the small subunit of bacteriophage λ terminase, alter the strength and specificity of holoterminase interactions with DNA. Virology. 231:1997;218-230.
    • (1997) Virology , vol.231 , pp. 218-230
    • Hwang, Y.1    Feiss, M.2
  • 34
    • 0026497522 scopus 로고
    • Site-directed mutagenesis of an amino acid residue in the bacteriophage P2 Ogr protein implicated in interaction with Escherichia coli RNA polymerase
    • King R. A., Anders D. L., Christie G. E. Site-directed mutagenesis of an amino acid residue in the bacteriophage P2 Ogr protein implicated in interaction with Escherichia coli RNA polymerase. Mol. Microbiol. 6:1992;3313-3320.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3313-3320
    • King, R.A.1    Anders, D.L.2    Christie, G.E.3
  • 35
    • 0024529497 scopus 로고
    • The interaction of E. coli integration host factor and lambda cos DNA multicomplex formation and protein-induced bending
    • Kosturko L., Daub E., Murialdo H. The interaction of E. coli integration host factor and lambda cos DNA multicomplex formation and protein-induced bending. Nucleic Acids Res. 17:1989;329-334.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 329-334
    • Kosturko, L.1    Daub, E.2    Murialdo, H.3
  • 36
    • 0028176499 scopus 로고
    • Chi sites in combination with RecA protein increase the survival of linear DNA in Escherichia coli by inactivating the ExoV activity of RecBCD nuclease
    • Kuzminov A., Schabtach E., Stahl F. W. Chi sites in combination with RecA protein increase the survival of linear DNA in Escherichia coli by inactivating the ExoV activity of RecBCD nuclease. EMBO J. 13:1994;2764-2776.
    • (1994) EMBO J. , vol.13 , pp. 2764-2776
    • Kuzminov, A.1    Schabtach, E.2    Stahl, F.W.3
  • 37
    • 0023042681 scopus 로고
    • Lambda phage protein Nu1 contains the conserved DNA binding fold of repressors
    • Kypr J., Mrazek J. Lambda phage protein Nu1 contains the conserved DNA binding fold of repressors. J. Mol. Biol. 91:1986;139-140.
    • (1986) J. Mol. Biol. , vol.91 , pp. 139-140
    • Kypr, J.1    Mrazek, J.2
  • 38
    • 0023127982 scopus 로고
    • Synthesis of a trans-acting inhibitor of DNA maturation by prohead mutants of phage λ
    • Murialdo H., Fife W. L. Synthesis of a trans-acting inhibitor of DNA maturation by prohead mutants of phage λ Genetics. 115:1987;3-10.
    • (1987) Genetics , vol.115 , pp. 3-10
    • Murialdo, H.1    Fife, W.L.2
  • 39
    • 0000340377 scopus 로고
    • P1 plasmid replication: Initiator sequestration is inadequate to explain control by initiator-binding sites
    • Pal S. K., Chattoraj D. K. P1 plasmid replication: Initiator sequestration is inadequate to explain control by initiator-binding sites. J. Bacteriol. 172:1988;2819-2824.
    • (1988) J. Bacteriol. , vol.172 , pp. 2819-2824
    • Pal, S.K.1    Chattoraj, D.K.2
  • 41
    • 0028200647 scopus 로고
    • The in vitro ATPases of bacteriophage lambda terminase and its large subunit, gene product A. The relationship with their DNA helicase and packaging activities
    • Rubinchik S., Parris W., Gold M. The in vitro ATPases of bacteriophage lambda terminase and its large subunit, gene product A. The relationship with their DNA helicase and packaging activities. J. Biol. Chem. 269:1994;13586-13593.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13586-13593
    • Rubinchik, S.1    Parris, W.2    Gold, M.3
  • 43
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP and GTP-binding proteins
    • Saraste M., Sibbald P., Wittinghofer A. The P-loop - A common motif in ATP and GTP-binding proteins. Trends Biochem. Sci. 15:1990;430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.2    Wittinghofer, A.3
  • 44
    • 0023818742 scopus 로고
    • The Nu1 subunit of bacteriophage lambda terminase binds to specific sites in cos DNA
    • Shinder G., Gold M. The Nu1 subunit of bacteriophage lambda terminase binds to specific sites in cos DNA. J. Virol. 62:1988;387-392.
    • (1988) J. Virol. , vol.62 , pp. 387-392
    • Shinder, G.1    Gold, M.2
  • 45
    • 0026567457 scopus 로고
    • Analysis of a mutation affecting the specificity domain for prohead binding of the bacteriophage lambda terminase
    • Sippy J., Feiss M. Analysis of a mutation affecting the specificity domain for prohead binding of the bacteriophage lambda terminase. J. Bacteriol. 174:1992;850-856.
    • (1992) J. Bacteriol. , vol.174 , pp. 850-856
    • Sippy, J.1    Feiss, M.2
  • 46
    • 0015579384 scopus 로고
    • Bacteriophage P4: A satellite virus depending on a helper such as prophage P2
    • Six E., Klug C. A. C. Bacteriophage P4: A satellite virus depending on a helper such as prophage P2. Virology. 51:1973;327-344.
    • (1973) Virology , vol.51 , pp. 327-344
    • Six, E.1    Klug, C.A.C.2
  • 47
    • 0020696370 scopus 로고
    • Isolation and characterization of P1 minireplicons, λ-P1:5R and λ-P1:5L
    • Sternberg N., Austin S. Isolation and characterization of P1 minireplicons, λ-P1:5R and λ-P1:5L. J. Bacteriol. 153:1983;800-812.
    • (1983) J. Bacteriol. , vol.153 , pp. 800-812
    • Sternberg, N.1    Austin, S.2
  • 48
    • 0027366175 scopus 로고
    • Kinetic characterization of the ATPase activity of the DNA packaging enzyme from bacteriophage lambda
    • Tomka M. A., Catalano C. E. Kinetic characterization of the ATPase activity of the DNA packaging enzyme from bacteriophage lambda. Biochemistry. 32:1993a;11992-11997.
    • (1993) Biochemistry , vol.32 , pp. 11992-11997
    • Tomka, M.A.1    Catalano, C.E.2
  • 49
    • 0027463091 scopus 로고
    • Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage lambda
    • Tomka M. A., Catalano C. E. Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage lambda. J. Biol. Chem. 268:1993b;3056-3065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3056-3065
    • Tomka, M.A.1    Catalano, C.E.2
  • 50
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira J. M. Production of single-stranded plasmid DNA. Methods Enzymol. 153:1987;3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.M.1
  • 51
    • 0000822783 scopus 로고
    • Preparative and analytical purification of DNA from agarose
    • Vogelstein B., Gillespie D. Preparative and analytical purification of DNA from agarose. Proc. Natl. Acad. Sci. USA. 76:1979;615-619.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 615-619
    • Vogelstein, B.1    Gillespie, D.2
  • 52
    • 0027318786 scopus 로고
    • Function of IHF in λ DNA packaging. II. Effects of mutations altering the IHF binding site and the intrinsic bend in cosB on λ development
    • Xin W., Cai Z.-H., Feiss M. Function of IHF in λ DNA packaging. II. Effects of mutations altering the IHF binding site and the intrinsic bend in cosB on λ development. J. Mol. Biol. 230:1993;505-515.
    • (1993) J. Mol. Biol. , vol.230 , pp. 505-515
    • Xin, W.1    Cai, Z.-H.2    Feiss, M.3
  • 53
    • 0024296540 scopus 로고
    • The interaction of Escherichia coli integration host factor with the cohesive end sites of phages lambda and 21
    • Xin W. N., Feiss M. The interaction of Escherichia coli integration host factor with the cohesive end sites of phages lambda and 21. Nucleic Acids Res. 16:1988;2015-2030.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2015-2030
    • Xin, W.N.1    Feiss, M.2
  • 54
    • 0027208111 scopus 로고
    • Function of IHF in λ DNA packaging. I. Identification of the strong binding site for integration host factor and the locus for intrinsic bending in cosB
    • Xin W., Feiss M. Function of IHF in λ DNA packaging. I. Identification of the strong binding site for integration host factor and the locus for intrinsic bending in cosB. J. Mol. Biol. 230:1993;492-504.
    • (1993) J. Mol. Biol. , vol.230 , pp. 492-504
    • Xin, W.1    Feiss, M.2
  • 55
    • 0025862034 scopus 로고
    • Structure of the bacteriophage lambda cohesive end site. Genetic analysis of the site (cosN) at which nicks are introduced by terminase
    • Xu S. Y., Feiss M. Structure of the bacteriophage lambda cohesive end site. Genetic analysis of the site (cosN) at which nicks are introduced by terminase. J. Mol. Biol. 220:1991;281-292.
    • (1991) J. Mol. Biol. , vol.220 , pp. 281-292
    • Xu, S.Y.1    Feiss, M.2
  • 56
    • 0030773016 scopus 로고    scopus 로고
    • Kinetic characterization of the strand separation ("helicase") activity of the DNA packaging enzyme from bacteriophage λ
    • Yang Q., Catalano C. E. C. Kinetic characterization of the strand separation ("helicase") activity of the DNA packaging enzyme from bacteriophage λ Biochemistry. 36:1997;10638-10645.
    • (1997) Biochemistry , vol.36 , pp. 10638-10645
    • Yang, Q.1    Catalano, C.E.C.2


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