메뉴 건너뛰기




Volumn 326, Issue 1, 2004, Pages 41-46

A fragile lattice: Replacing bacteriophage λ's head stability gene D with the shp gene of phage 21 generates the Mg 2+-dependent virus, λ shp

Author keywords

Chimeras; Phage head stability; Virion stability; Virus assembly; Virus shell

Indexed keywords

MAGNESIUM ION;

EID: 3242673586     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2004.05.024     Document Type: Article
Times cited : (17)

References (22)
  • 1
    • 0001944551 scopus 로고
    • Experimental methods for use with lambda
    • R. Hendrix, J. Roberts, F. Stahl, & R. Weisberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arber W., Enquist B., Hohn N., Murray E., Murray K. Experimental methods for use with lambda. Hendrix R., Roberts J., Stahl F., Weisberg R. Lambda II. 1983;366-433 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1983) Lambda II , pp. 366-433
    • Arber, W.1    Enquist, B.2    Hohn, N.3    Murray, E.4    Murray, K.5
  • 2
    • 0001035136 scopus 로고
    • Complete annotated lambda sequence
    • R. Hendrix, J. Roberts, F. Stahl, & R. Weisberg. Cold pring Harbor: Cold Spring Harbor Laboratory Press
    • Daniels D., Schroeder J., Szybalski W., Sanger F., Coulsen A. Complete annotated lambda sequence. Hendrix R., Roberts J., Stahl F., Weisberg R. Lambda II. 1983;519-676 Cold Spring Harbor Laboratory Press, Cold pring Harbor
    • (1983) Lambda II , pp. 519-676
    • Daniels, D.1    Schroeder, J.2    Szybalski, W.3    Sanger, F.4    Coulsen, A.5
  • 3
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K., Wanner B. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 2000;6640-6645
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , pp. 6640-6645
    • Datsenko, K.1    Wanner, B.2
  • 4
    • 0042326090 scopus 로고    scopus 로고
    • Mechanism of scaffolding-assisted viral assembly
    • Fane B.A., Prevelige P.E. Jr. Mechanism of scaffolding-assisted viral assembly. Adv. Protein Chem. 64:2003;259-299
    • (2003) Adv. Protein Chem. , vol.64 , pp. 259-299
    • Fane, B.A.1    Prevelige Jr., P.E.2
  • 6
    • 0024819017 scopus 로고
    • Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography
    • Furcinitti P.S., van Oostrum J., Burnett R.M. Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography. EMBO J. 8:1989;3563-3570
    • (1989) EMBO J. , vol.8 , pp. 3563-3570
    • Furcinitti, P.S.1    Van Oostrum, J.2    Burnett, R.M.3
  • 7
    • 0018258320 scopus 로고
    • Specificity determinants for bacteriophage lambda DNA replication: I. A chain of interactions that controls the initiation of replication
    • Furth M.E., McLeester C., Dove W.F. Specificity determinants for bacteriophage lambda DNA replication: I. A chain of interactions that controls the initiation of replication. J. Mol. Biol. 126:1978;195-225
    • (1978) J. Mol. Biol. , vol.126 , pp. 195-225
    • Furth, M.E.1    McLeester, C.2    Dove, W.F.3
  • 8
  • 9
    • 0017597092 scopus 로고
    • The two dispensable structural proteins (soc and hoc) of the T4 phage capsid: Their properties, isolation and characterization of defective mutants, and their binding with the defective heads in vitro
    • Ishii T., Yanagida M. The two dispensable structural proteins (soc and hoc) of the T4 phage capsid: their properties, isolation and characterization of defective mutants, and their binding with the defective heads in vitro. J. Mol. Biol. 109:1977;487-514
    • (1977) J. Mol. Biol. , vol.109 , pp. 487-514
    • Ishii, T.1    Yanagida, M.2
  • 10
    • 0030582396 scopus 로고    scopus 로고
    • Surface display of proteins on bacteriophage λ heads
    • Mikawa Y.G., Maruyama I., Brenner S. Surface display of proteins on bacteriophage λ heads. J. Mol. Biol. 262:1996;21-30
    • (1996) J. Mol. Biol. , vol.262 , pp. 21-30
    • Mikawa, Y.G.1    Maruyama, I.2    Brenner, S.3
  • 11
    • 0016776711 scopus 로고
    • Model for arrangement of minor structural proteins in head of bacteriophage lambda
    • Murialdo H., Ray P. Model for arrangement of minor structural proteins in head of bacteriophage lambda. Nature. 257:1975;815-817
    • (1975) Nature , vol.257 , pp. 815-817
    • Murialdo, H.1    Ray, P.2
  • 12
    • 0011140369 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Sambrook J., Fritsch E., Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed.:1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (1989) 2nd Ed.
    • Sambrook, J.1    Fritsch, E.2    Maniatis, T.3
  • 13
    • 0024552611 scopus 로고
    • Three-dimensional structure of the HSV1 nucleocapsid
    • Schrag J.D., Prasad B.V., Rixon F.J., Chiu W. Three-dimensional structure of the HSV1 nucleocapsid. Cell. 56:1989;651-660
    • (1989) Cell , vol.56 , pp. 651-660
    • Schrag, J.D.1    Prasad, B.V.2    Rixon, F.J.3    Chiu, W.4
  • 15
    • 0002598437 scopus 로고
    • Heteroduplexes of DNA molecules of lambdoid phages: Physical mapping of their base sequence relationships by electro microscopy
    • A.D. Hershey. Cold Spring Harbor: Cold Spring Harbor Press
    • Simon M.N., Davis R.W., Davidson N. Heteroduplexes of DNA molecules of lambdoid phages: Physical mapping of their base sequence relationships by electro microscopy. Hershey A.D. The Bacteriophage Lambda. 1971;313-328 Cold Spring Harbor Press, Cold Spring Harbor
    • (1971) The Bacteriophage Lambda , pp. 313-328
    • Simon, M.N.1    Davis, R.W.2    Davidson, N.3
  • 16
    • 0027522436 scopus 로고
    • Sequence analysis of the phage 21 genes for prohead assembly and head completion
    • Smith M., Feiss M. Sequence analysis of the phage 21 genes for prohead assembly and head completion. Gene. 126:1993;1-7
    • (1993) Gene , vol.126 , pp. 1-7
    • Smith, M.1    Feiss, M.2
  • 17
    • 0028907327 scopus 로고
    • Display of peptides and proteins on the surface of bacteriophage λ
    • Sternberg N., Hoess R. Display of peptides and proteins on the surface of bacteriophage λ Proc. Natl. Acad. Sci. U.S.A. 92:1995;1609-1613
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1609-1613
    • Sternberg, N.1    Hoess, R.2
  • 18
    • 0017596750 scopus 로고
    • Packaging of coliphage lambda DNA: II. The role of the gene D protein
    • Sternberg N., Weisberg R. Packaging of coliphage lambda DNA: II. The role of the gene D protein. J. Mol. Biol. 117:1977;733-759
    • (1977) J. Mol. Biol. , vol.117 , pp. 733-759
    • Sternberg, N.1    Weisberg, R.2
  • 19
    • 0027085892 scopus 로고
    • Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, co-operativity, and super-stabilization by soc binding
    • Steven A.C., Greenstone H.L., Booy F.P., Black L.W., Ross P.D. Conformational changes of a viral capsid protein. Thermodynamic rationale for proteolytic regulation of bacteriophage T4 capsid expansion, co-operativity, and super-stabilization by soc binding. J. Mol. Biol. 228:1992;870-884
    • (1992) J. Mol. Biol. , vol.228 , pp. 870-884
    • Steven, A.C.1    Greenstone, H.L.2    Booy, F.P.3    Black, L.W.4    Ross, P.D.5
  • 20
    • 0029908793 scopus 로고
    • The herpes simplex virus procapsid: Structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R., Steven A.C. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263:1992;447-462
    • (1992) J. Mol. Biol. , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6    Steven, A.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.