Literature DB >> 8503175

Bacteriophage PRD1 proteins: cross-linking and scanning transmission electron microscopy analysis.

C Luo1, J Hantula, W Tichelaar, D H Bamford.   

Abstract

Bacteriophage PRD1, a double-stranded DNA virus infecting Escherichia coli, has a membrane inside the protein capsid. Chemical cross-linking and scanning transmission electron microscopy showed that the multimeric major coat protein (P3) exists in a trimeric form. Cross-linking revealed, in addition, that protein P11, located between the protein coat and the membrane, exists also as a homotrimer. Minor protein P7 was associated with the major coat protein P3. Under nonreducing conditions the infectivity proteins P16 and P18 formed homomultimeric complexes which were dissociated upon addition of 2-mercaptoethanol.

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Year:  1993        PMID: 8503175     DOI: 10.1006/viro.1993.1296

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  2 in total

1.  Functional organization of the bacteriophage PRD1 genome.

Authors:  A M Grahn; J K Bamford; M C O'Neill; D H Bamford
Journal:  J Bacteriol       Date:  1994-05       Impact factor: 3.490

2.  DNA packaging orders the membrane of bacteriophage PRD1.

Authors:  S J Butcher; D H Bamford; S D Fuller
Journal:  EMBO J       Date:  1995-12-15       Impact factor: 11.598

  2 in total

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