Bacteriophage Lambda Terminase and the Mechanism of Viral DNA Packaging (original) (raw)

• Katsura I. Tail assembly and injection. In: Hendrix RW, Roberts JW, Stahl FW et al, eds. Lambda II. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1983:331–346.
  Google Scholar
• Hendrix RW, Roberts JW, Stahl FW et al. Lambda II. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1983.
  Google Scholar
• Herskowitz I, Hagen D. The lysis-lysogeny decision of phage lambda: Explicit programming and responsiveness. Ann Rev Genetics 1980; 14:399–445.
  Article CAS Google Scholar
• Ptashne M, Gann A. Genes & Signals. Cold Spring Harbor: Cold Spring Harbor Press, 2001.
  Google Scholar
• Friedman D, Gottesman M. Lytic mode of lambda development. In: Hendrix RW, Roberts JW, Stahl FW et al, eds. “Lambda IT”. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1983:21–51.
  Google Scholar
• Higgins RR, Lucko HJ, Becker A. Mechanism of cos DNA cleavage by bacteriophage lambda terminase: Multiple roles of ATP. Cell 1988; 54(6):765–75.
  Article PubMed CAS Google Scholar
• 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 1994; 269(18):13586–93.
  PubMed CAS Google Scholar
• Rubinchik S, Parris W, Gold M. The in vitro translocase activity of lambda terminase and its subunits. Kinetic and biochemical analysis. J Biol Chem 1995; 270(34):20059–66.
  Article PubMed CAS Google Scholar
• Woods L, Catalano C. Kinetic characterization of the GTPase activity of phage lambda terminase: Evidence for communication between the two “NTPase” catalytic sites of the enzyme. Biochemistry 1999; 38:4624–4630.
  Article CAS Google Scholar
• Woods L, Terpening C, Catalano CE. Kinetic analysis of the endonuclease activity of phage lambda terminase: Assembly of a catalytically competent nicking complex is rate-limiting. Biochemistry 1997; 36(19):5777–85.
  Article PubMed CAS Google Scholar
• Cue D, Feiss M. Bacteriophage λ DNA packaging: DNA site requirements for termination and processivity. J Mol Biol 2001; 311:233–240.
  Article PubMed CAS Google Scholar
• Feiss M, Kobayashi I, Widner W. Separate sites for binding and nicking of bacteriophage lambda DNA by terminase. Proc Natl Acad Sci USA 1983; 80(4):955–9.
  Article PubMed CAS Google Scholar
• Feiss M, Widner W, Miller G et al. Structure of the bacteriophage lambda cohesive end site: Location of the sites of terminase binding (cosB) and nicking (cosN). Gene 1983; 24(2–3):207–18.
  Article PubMed CAS Google Scholar
• Hohn B. DNA sequences necessary for packaging of bacteriophage λ DNA. Proc Nat Acad Sci USA 1983; 80:7456–7460.
  Article PubMed CAS Google Scholar
• Miwa T, Matsubara K. Lambda phage DNA sequences affecting the packaging process. Gene 1983; 24:199–206.
  Article PubMed CAS Google Scholar
• Cue D, Feiss M. A site required for termination of packaging of the phage lambda chromosome. Proc Natl Acad Sci USA 1993b; 90(20):9290–4.
  Article PubMed CAS Google Scholar
• 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 1992; 161:305–315.
  Article Google Scholar
• 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 1993a; 234(3):594–609.
  Article PubMed CAS Google Scholar
• Higgins RR, 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 1994a; 13(24):6152–61.
  PubMed CAS Google Scholar
• 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 1993; 230:492–504.
  Article PubMed CAS Google Scholar
• Yeo A, Feiss M. Specific interaction of terminase, the DNA packaging enzyme of bacteriophage lambda, with the portal protein of the prohead. J Mol Biol 1995; 245(2):141–50.
  Article PubMed CAS Google Scholar
• 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 1997; 147:7–17.
  PubMed CAS Google Scholar
• Wieczorek D, Didion L, Feiss M. Alterations of the portal protein of bacteriophage λ suppress mutations in cosQ, the site required for termination of DNA packaging. Submitted Genetics 2002; 161:21–31.
  CAS Google Scholar
• Wieczorek D, Feiss M. Defining cosQ, the site required for termination of bacteriophage lambda DNA packaging. Genetics 2001; 158:495–506.
  PubMed CAS Google Scholar
• Wieczorek D, Feiss M. Genetics of cosQ, the DNA packaging termination site of phage λ: A study of local suppression and methylation effects. Genetics 2003; In press.
  Google Scholar
• Cue D, Feiss M. Termination of packaging of the bacteriophage lambda chromosome: cosQ is required for nicking the bottom strand of cosN. J Mol Biol 1998; 280(1):11–29.
  Article PubMed CAS Google Scholar
• Miller G, Feiss M. The bacteriophage lambda cohesive end site: Isolation of spacing/substitution mutations that result in dependence on Escherichia coli integration host factor. Mol Gen Genet 1988; 212(1):157–65.
  Article PubMed CAS Google Scholar
• Goodrich JA, Schwartz ML, McClure WR. Searching for and predicting the activity of sites for DNA binding proteins: Compilation and analysis of the binding sites for Escherichia coli integration host factor (IHF). Nucleic Acids Res 1990; 18:4993–5000.
  Article PubMed CAS Google Scholar
• Mendelson I, Gottesman M, Oppenheim AB. HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase. J Bact 1991; 173:1670–1676.
  PubMed CAS Google Scholar
• Higgins RR, 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 1994b; 13(24):6162–71.
  PubMed CAS Google Scholar
• Tomka MA, Catalano CE. Physical and kinetic characterization of the DNA packaging enzyme from bacteriophage lambda. J Biol Chem 1993b; 268(5):3056–65.
  PubMed CAS Google Scholar
• Yang Q, Hanagan A, Catalano CE. Assembly of a nucleoprotein complex required for DNA packaging by bacteriophage lambda. Biochemistry 1997; 36(10):2744–52.
  Article PubMed CAS Google Scholar
• Shinder G, Gold M. The Nu1 subunit of bacteriophage lambda terminase binds to specific sites in cos DNA. J Virology 1988; 62:387–392.
  PubMed CAS Google Scholar
• Parris W, Rubinchik S, Yang YC et al. A new procedure for the purification of the bacteriophage lambda terminase enzyme and its subunits. Properties of gene product A, the large subunit. J Biol Chem 1994; 269(18):13564–74.
  PubMed CAS Google Scholar
• Smith MP, Feiss M. Sequence analysis of the phage 21 genes for prohead assembly and head completion. Gene 1993a; 126(1): 1–7.
  Article PubMed CAS Google Scholar
• Smith MP, Feiss M. Sites and gene products involved in lambdoid phage DNA packaging. J Bacteriol 1993b; 175(8):2393–9.
  PubMed CAS Google Scholar
• Siegele DA, Frackman S, Sippy J et al. The head genes of bacteriophage 21. Virology 1983; 129(2):484–9.
  Article PubMed CAS Google Scholar
• Frackman S, Siegele DA, Feiss M. A functional domain of bacteriophage lambda terminase for prohead binding. J Mol Biol 1984; 180(2):283–300.
  Article PubMed CAS Google Scholar
• Frackman S, Siegele DA, Feiss M. The terminase of bacteriophage lambda. Functional domains for cosB binding and multimer assembly. J Mol Biol 1985; 183(2):225–38.
  Article PubMed CAS Google Scholar
• Wu WF, Christiansen S, Feiss M. Domains for protein-protein interactions at the N and C termini of the large subunit of bacteriophage lambda terminase. Genetics 1988; 119(3):477–84.
  PubMed CAS Google Scholar
• Yang Q, Beer TD, Woods L et al. Cloning, expression, and characterization of a DNA binding domain of gpNu1, a phage lambda DNA packaging protein. Biocemistry 1999a; 38:465–477.
  CAS Google Scholar
• Yang Q, Berton N, Manning M et al. Domain structure of gpNu1, a phage lambda DNA packaging protein. Biochemistry 1999b; 38:14238–14447.
  Article PubMed CAS Google Scholar
• de Beer T, Meyer J, Ortega M et al. Insights into specific DNA recognition during assembly of a viral genome packaging machine; structure and genetics of the DNA binding domain of gpNu1. Molecular Cell 2002; 9:981–991.
  Article PubMed Google Scholar
• Bain D, Berton N, Ortega M et al. Biophysical characterization of the DNA binding domain of gpNu1, a viral DNA packaging protein. J Biol Chem 2001; 276:20175–20181.
  Article PubMed CAS Google Scholar
• Becker A. (cited in Feiss, M). Terminase and the recognition, cutting and packaging of λ chromosomes. Trends Genet 1986; 2:100–104.
  Article Google Scholar
• Feiss M. Terminase and the recognition, cutting and packaging of λ chromosomes. Trends Genet 1986; 2:100–104.
  Article CAS Google Scholar
• Kypr J, Mrazek J. Lambda phage protein Nu1 contains the conserved DNA binding fold of repressors. J Mol Biol 1986; 91:139–140.
  Article Google Scholar
• Clark K, Halay E, Lai E et al. Cocrystal structure of HNF-3/forkhead DNA-recognition motif resembles histone H5. Nature 1993; 364:412–420.
  Article PubMed CAS Google Scholar
• Weigel D, Jackie H. The fork head domain: A novel DNA binding motif of eukaryotic transcription factors. Cell 1990; 63:455–456.
  Article PubMed CAS Google Scholar
• Martinez-Hackert E, Stock A. Structural relationshiip in the OmpR family of winged-helix transcription factors. J Mol Biol 1997; 269:301–312.
  Article PubMed CAS Google Scholar
• Clubb R, Omichinski J, Savilahti H et al. A novel class of winged helix-turn-helix protein: The DNA-binding domain of Mu transposase. Structure 1994; 2:1041–1048.
  Article PubMed CAS Google Scholar
• Ilangovan U, Wojciak J, Connolly K et al. NMR structure and functional studies of the Mu repressor DNA binding domain. Biochemistry 1999; 38:8367–8376.
  Article PubMed CAS Google Scholar
• Wintjens R, Rooman M. Structural classification of HTH DNA-binding domains and protein-DNA interaction modes. J Mol Biol 1996; 262:294–313.
  Article PubMed CAS Google Scholar
• Gussin G, Johnson A, Pabo C et al. Repressor and cro protein: Structure, function, and role in Lysogenization. In: Hendrix RW, Roberts JW, Stahl FW et al, eds. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1983:93–120.
  Google Scholar
• Bear S, Court D, Friedman D. An accessory role for Escherichia coli integration host factor: Characterization of a lambda mutant dependent upon integration host factor for DNA packaging. J Virol 1984; 52:966–972.
  PubMed CAS Google Scholar
• Kosturko L, Daub E, Murialdo H. The interaction of E. coli intergration host factor and lambda cos DNA multicomplex formation and protein-induced bending. Nucleic Acids Res 1989; 17:329–334.
  Article Google Scholar
• Rice PA, Yang S, Mizuuchi K et al. Crystal structure of an IHF-DNA complex: A protein-induced DNA U-turn. Cell 1996; 87(7):1295–306.
  Article PubMed CAS Google Scholar
• Friedman D. Integration host factor: A protein for all reasons. Cell 1988; 55:545–549.
  Article PubMed CAS Google Scholar
• 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 1993; 230:505–515.
  Article PubMed CAS Google Scholar
• Hwang Y, Feiss M. A defined system for in vitro lambda DNA packaging. Virology 1995; 211(2):367–76.
  Article PubMed CAS Google Scholar
• Yang Q, Catalano C. Biochemical characterization of bacteriophage lambda genome packaging in vitro. Virology 2003; 305:276–287.
  Article PubMed CAS Google Scholar
• Cue D, Feiss M. Genetic analysis of cosB, the binding site for terminase, the DNA packaging enzyme of bacteriophage lambda. J Mol Biol 1992a; 228(1):58–71.
  Article PubMed CAS Google Scholar
• Cue D, Feiss M. Genetic analysis of mutations affecting terminase, the bacteriophage lambda DNA packaging enzyme, that suppress mutations in cosB, the terminase binding site. J Mol Biol 1992b; 228(1):72–87.
  Article PubMed CAS Google Scholar
• Granston AE, Alessi DM, Eades L et al. A point mutation in the Nu1 gene of bacteriophage λ facilitates phage growth in Escherichia coli with himA and gyrB mutations. Mol Gen Genet 1988; 212:149–156.
  Article PubMed CAS Google Scholar
• Yeo A, Kosturko LD, Feiss M. Structure of the bacteriophage lambda cohesive end site: Bent DNA on both sides of the site, cosN, at which terminase introduces nicks during chromosome maturation. Virology 1990; 174(1):329–34.
  Article PubMed CAS Google Scholar
• Sippy J, Feiss M. Analysis of a mutation affecting the specificity domain for prohead binding of the bacteriophage lambda terminase. J Bacteriol 1992; 174(3):850–6.
  PubMed CAS Google Scholar
• Hwang Y, Catalano CE, Feiss M. Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage λ. Biochemistry 1996; 35(8):2796–803.
  Article PubMed CAS Google Scholar
• Saraste M, Sibbald P, Wittinghofer A. The P-loop — A common motif in ATP and GTP-binding proteins. Trends in Biochemical Sciences 1990; 15:430–434.
  Article PubMed Google Scholar
• Walker JE, Saraste M, Runswick MJ et al. Distantly 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 1982b; 8:945–951.
  Google Scholar
• Tomka MA, Catalano CE. Kinetic characterization of the ATPase activity of the DNA packaging enzyme from bacteriophage lambda. Biochemistry 1993a; 32(45):11992–7.
  Article PubMed CAS Google Scholar
• Guo P, Peterson C, Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage Ф29. J Mol Biol 1987; 197:229–236.
  Article PubMed CAS Google Scholar
• 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 1996; 261(4):524–35.
  Article PubMed CAS Google Scholar
• Hwang Y, Feiss M. The endonuclease and helicase activities of Bacteriophage λ? terminase: Changing nearby residue 515 restores activity to the gpA K497D mutant enzyme. Virology 2000; 277:204–214.
  Article PubMed CAS Google Scholar
• Duffy C, Feiss M. The large subunit of bacteriophage lambda’s terminase plays a role in DNA translocation and packaging termination. J Mol Biol 2002; 316:547–561.
  Article PubMed CAS Google Scholar
• Hang Q, Tack B, Feiss M. An ATPase center of bacteriophage λ terminase involved in post-cleavage stages of DNA packaging: Identification of ATP-interactive amino acids. J Mol Biol 2000; 302:777–795.
  Article PubMed CAS Google Scholar
• Pu W, Struhl K. The leucine zipper symmetrically positions the adjacent basic regions for specific DNA binding. Proc Nat Acad Sci USA 1991; 88:6901–6905.
  Article PubMed CAS Google Scholar
• Dhar A, Feiss M. Mutations in the ATP reactive center of λ terminase and its effect on DNA packaging. Unpublished observations 2003.
  Google Scholar
• Mitchell M, Matsuzaki S, Imai S et al. Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Res 2002; 30:4009–4021.
  Article PubMed CAS Google Scholar
• Rao V, Mitchell M. The N-terminal ATPase site in the large terminase protein Gp17 is critically required for DNA packaging in bacteriophage T4. J Mol Biol 2001; 314:411–421.
  Article CAS Google Scholar
• Gorbalenya A, Koonin E. Curr Opin Struct Biol 1993; 3:419–429.
  Article CAS Google Scholar
• Story R, Li H, Abelson J. Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc Natl Acad Sci USA 2001; 98:14650–1470.
  Article Google Scholar
• Yang Q, Catalano C. A minimal kinetic model for a viral DNA packaging machine. Biochemistry 2004; 43:289–299.
  Article PubMed CAS Google Scholar
• Hang J, Catalano C, Feiss M. The functional asymmetry of cosN, the nicking site for bacterioph age λ DNA packaging, is dependent on the terminase binding site, cosB. Biochemistry 2001; 40:13370–13377.
  Article PubMed CAS Google Scholar
• Xu SY, 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 1991; 220(2):281–92.
  Article PubMed CAS Google Scholar
• Yang Q, Catalano CE. Kinetic characterization of the strand separation (“helicase”) activity of the DNA packaging enzyme from bacteriophage λ. Biochemistry 1997; 36:10638–10645.
  Article PubMed CAS Google Scholar
• Delagoutte E, Hippel PV. Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: Structures and properties of isolated helicases. Quart Rev Biophys 2002; 35:431–478.
  Article CAS Google Scholar
• Lohman T. Helicase-catalyzed DNA unwinding. J Biol Chem 1993; 268:2269–2272.
  PubMed CAS Google Scholar
• Patel S, Picha K. Structure and function of hexameric helicases. Ann Rev Biochem 2000; 69:651–697.
  Article PubMed CAS Google Scholar
• Becker A, Murialdo H, Gold M. Studies on an in vitro system for the packaging and maturation of phage λ DNA. Virology 1977; 78:277–290.
  Article PubMed CAS Google Scholar
• Becker A, Gold M. Prediction of an ATP reactive center in the small subunit, gpNu1, of the phage lambda terminase enzyme. J Mol Biol 1988; 199(1):219–22.
  Article PubMed CAS Google Scholar
• Babbar BK, Gold M. ATP-reactive sites in the bacteriophage λ packaging protein terminase lie in the N-termini of its subunits, gpA and gpNu1. Virology 1998; 247:251–264.
  Article PubMed CAS Google Scholar
• Catalano C, Woods L. Kinetic characterization of the GTPase activity of phage lambda terminase: Evidence for communication between the two “NTPase” catalytic sites of the enzyme. Biochemistry 1999; 38:4624–4630.
  Google Scholar
• Catalano C. The terminase enzyme from bacteriophage lambda: A DNA-packaging machine. Cell Mol Life Sci 2000; 57:128–148.
  Article PubMed CAS Google Scholar
• Catalano CE, Cue D, Feiss M. Virus DNA packaging: The strategy used by phage lambda. Mol Microbiol 1995; 16(6):1075–86, [Review] [87 refs].
  Article PubMed CAS Google Scholar
• Georgopoulos C, Tilly K, Casjens S. Lambdoid phage head assembly. In: Hendrix RW, Roberts JW, Stahl FW et al, eds. Lambda II. Cold Spring Harbor: Cold Spring Harbor Press, 1983:279–304.
  Google Scholar
• Kochan J, Carrascosa JL, Murialdo H. Bacteriophage lambda preconnectors: Purification and structure. J Mol Biol 1984; 174:433–447.
  Article PubMed CAS Google Scholar
• Walker JE, Aufferet AD, Carne A et al. Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels: An aid to interpretation of DNA sequences as exemplified by Escherichia coli unc operon and bacteriophage lambda. Eur J Biochem 1982a; 123:23–260.
  Article Google Scholar
• Hendrix R, Casjens S. Locations and amounts of major structural proteins in bacteriophage lambda. J Mol Biol 1974a; 88:535–545.
  Article PubMed Google Scholar
• Hohn B. DNA as substrate for packaging into phage lambda in vitro. J Mol Biol 1975; 98:93–106.
  Article PubMed CAS Google Scholar
• Hendrix RW, Casjens SR. Protein fusion during the assembly of phage lambda heads. Journal of Supramolecular Structure 1974b; 2(2–4):329–36.
  Article PubMed CAS Google Scholar
• Hendrix RW, Casjens SR. Protein fusion: A novel reaction in bacteriophage lambda head assembly. Proc Natl Acad Sci USA 1974c; 71(4): 1451–5.
  Article PubMed CAS Google Scholar
• Hohn T, Hohnl F. Petit lambda, a family of particles from coliphage lambda-infected cells. J Mol Biol 1975; 98:107–120.
  Article PubMed CAS Google Scholar
• Baird L, Lipinska B, Raina S et al. Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype. J Bacteriol 1991; 173:5763–70.
  PubMed CAS Google Scholar
• Hendrix RW, Casjens SR. Assembly of bacteriophage lambda heads: Protein processing and its genetic control in petit lambda assembly. J Mol Biol 1975; 91(2): 187–99.
  Article PubMed CAS Google Scholar
• Higgins RR, Becker A. Interaction of terminase, the DNA packaging enzyme of phage lambda, with its cos DNA substrate. J Mol Biol 1995; 252(1):31–46.
  Article PubMed CAS Google Scholar
• Becker A, Murialdo H, Gold M. Early events in the in vitro packaging of bacteriophage DNA. Virology 1977; 78:291–305.
  Article PubMed CAS Google Scholar
• Murialdo H, Fife W. The maturation of coliphage lambda DNA in the absence of its packaging. Gene 1984; 30:183–194.
  Article PubMed CAS Google Scholar
• Sippy J, Feiss M. Initial cos cleavage of bacteriophage λ concatemers requires proheads and gpFI in vivo. Mol Microbiol 2004; In press.
  Google Scholar
• Emmons SW. Bacteriophage lambda derivatives carrying two copies of the cohesive end site. J Mol Biol 1974; 83(4):511–25.
  Article PubMed CAS Google Scholar
• Kuzminov A, Schabtach E, Stahl FW. 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 1994; 13:2764–2776.
  PubMed CAS Google Scholar
• Borukhov S, Severinov K. Role of the RNA polymerase sigma subunit in transcription initiation. Res Microbiology 2002; 153:557–562.
  Article CAS Google Scholar
• Murialdo H, Tzamtzis D. Mutations of the coat protein gene of bacteriophage λ that overcome the necessity for the FI gene. The EFi domain. Mol Microbiol 1997; 24:341–53.
  Article PubMed CAS Google Scholar
• Murialdo H, Tzamtzis D, Berru M et al. Mutations in the terminase genes of bacteriophage λ that bypass the necessity for FI. Mol Microbiol 1997; 24:937–952.
  Article PubMed CAS Google Scholar
• MacKinlay AG, Kaiser AD. DNA replication in head mutants of bacteriophage?λ. J Mol Biol 1969; 39:679–683.
  Article PubMed CAS Google Scholar
• Wake R, Kaiser A, Inman R. Isolation and structure of phage lambda head-mutant DNA. J Mol Biol 1972; 64:519–540.
  Article PubMed CAS Google Scholar
• Murialdo H, Fife WL. Synthesis of a trans-acting inhibitor of DNA maturation by prohead mutants of phage λ. Genetics 1987; 115:3–10.
  PubMed CAS Google Scholar
• Becker A, Murialdo H, Lucko H et al. Bacteriophage lambda DNA packaging. The product of the FI gene promotes the incorporation of the prohead to the DNA-terminase complex. J Mol Biol 1988; 199(4):597–607.
  Article PubMed CAS Google Scholar
• Becker A, Gold A. Enzymatic breakage of the cohesive end site of phage lambda DNA: Terminase (ter) reaction. Proc Natl Acad Sci USA 1978; 4199–4203 (75).
  Article PubMed CAS Google Scholar
• Chow S, Daub E, Murialdo H. The overproduction of DNA terminase of coliphage lambda. Gene 1987; 60:277–289.
  Article PubMed CAS Google Scholar
• Catalano CE, Tomka MA. Role of gpFI protein in DNA packaging by bacteriophage lambda. Biochemistry 1995; 34(31):10036–42.
  Article PubMed CAS Google Scholar
• Cai Z-H, Hwang Y, Cue D et al. Mutations in Nu1, the gene encoding the small subunit of bacteriophage? λ??terminase, suppress the postcleavage DNA packaging defect of cosB mutations. J Bacteriol 1997; 179:2479–2485.
  PubMed CAS Google Scholar
• Pruss G, Calendar R. Maturation of bacteriophage P2 DNA. Virology 1978; 86:454–467.
  Article PubMed CAS Google Scholar
• Chai S, Bravo A, Luder G et al. Molecular analysis of the Bacillus subtilis bacteriophage SPP1 region encompassing genes 1 to 6. The products of gene 1 and gene 2 are required for pac cleavage. J Mol Biol 1992; 224:87–102.
  Article PubMed CAS Google Scholar
• Laski F, Jackson E. Maturation cleavage of bacteriophage P22 DNA in the absence of DNA packaging. J Mol Biol 1982; 154:565–79.
  PubMed CAS Google Scholar
• Davidson A, Gold M. A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage λ FI gene product. Virology 1987; 161:305–315.
  Article PubMed CAS Google Scholar
• Murialdo H, Fife W, Becker A et al. Bacteriophage lambda DNA maturation. The functional relationships among the products of genes Nu1, A and FI. J Mol Biol 1981; 145(2):375–404.
  Article PubMed CAS Google Scholar
• Lin H, Simon M, Black L. Purification and characterization of the small subunit of phage T4 terminase, gp16, required for DNA packaging. J Biol Chem 1997; 272:3495–3501.
  Article PubMed CAS Google Scholar
• Lurz R, Orlova E, Gunther D et al. Structural organisation of the head-to-tail interface of a bacterial virus. J Mol Biol 2001; 310:1027–1037.
  Article PubMed CAS Google Scholar
• Fujisawa H, Shibata H, Kato H. Analysis of interactions among factors involved in the bacteriophage T3 DNA packaging reaction in a defined in vitro system. Virology 1991; 185:788–794.
  Article PubMed CAS Google Scholar
• Fujisawa H, Morita M. Phage DNA packaging. Genes to Cells 1997; 2:537–545.
  Article PubMed CAS Google Scholar
• Schliwa M, Woelke G. Molecular motors. Nature 2003; 422:759–765.
  Article PubMed CAS Google Scholar
• Earnshaw WC, Casjens SR. DNA packaging by the double-stranded DNA bacteriophages. Cell 1980; 21(2):319–31.
  Article PubMed CAS Google Scholar
• Hendrix R. Symmetry mismatch and DNA packaging in large bacteriophages. Proc Natl Acad Sci USA 1978; 75:4779–4793.
  Article PubMed CAS Google Scholar
• Simpson A, Tao Y, Leiman P et al. Structure of the bacteriophage phi29 DNA packaging motor. Nature 2000; 408:745–750.
  Article PubMed CAS Google Scholar
• Serwer P. Models of bacteriophage DNA packaging motors. J Struct Biol 2003; 141:179–188.
  Article PubMed CAS Google Scholar
• Dokland T, Murialdo H. Structural transitions during maturation of bacteriophage lambda capsids. J Mol Biol 1993; 233(4):682–94.
  Article PubMed CAS Google Scholar
• Murialdo H. Bacteriophage lambda DNA maturation and packaging. Ann Rev Biochem 1991; 60:125–153.
  Article PubMed CAS Google Scholar
• Imber R, Tsugita A, Wurtz M et al. Outer surface protein of bacteriophage lambda. J Mol Biol 1980; 139(3):277–95.
  Article PubMed CAS Google Scholar
• Perucchetti R, Parris W, Becker A et al. Late stages in bacteriophage lambda head morphogenesis: In vitro studies on the action of the bacteriophage lambda D-gene and W-gene products. Virology 1988; 165(1):103–14.
  Article PubMed CAS Google Scholar
• Sternberg N, Weisberg R. Packaging of coliphage lambda DNA: II. the role of the gene D protein. J Mol Biol 1977; 117:733–759.
  Article PubMed CAS Google Scholar
• Wendt J, Feiss M. A fragile lattice: Replacing bacteriophage?λ’s head stability gene D with the shp gene of phage 21 generates the Mg++-dependent virus, λ, shp. Virology 2004; 326:41–46.
  Article PubMed CAS Google Scholar
• Smith D, Tans S, Smith S et al. The bacteriophage phi29 portal motor can package DNA against a large internal force. Nature 2001; 413:748–52.
  Article PubMed CAS Google Scholar
• Casjens S, Wyckoff E, Hayden M et al. Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA. J Mol Biol 1992; 224(4): 1055–74.
  Article PubMed CAS Google Scholar
• Tavares P, Santos MA, Lurz R et al. Identification of a gene in Bacillus subtilis bacteriophage SPP1 determining the amount of packaged DNA. J Mol Biol 1992; 225(1):81–92.
  Article PubMed CAS Google Scholar
• Casjens S. Bacteriophage lambda FII gene protein: Role in head assembly. J Mol Biol 1974; 90:1–20.
  Article PubMed CAS Google Scholar
• Maxwell K, Yee A, Booth V et al. The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold. J Mol Biol 2001; 308:9–14.
  Article PubMed CAS Google Scholar
• Maxwell K, Yee A, Arrowsmith C et al. The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. J Mol Biol 2002; 318:1395–1404.
  Article PubMed CAS Google Scholar