A trans-envelope protein complex needed for filamentous phage assembly and export.
Assembly and export of filamentous phage requires four non-capsid proteins: the outer membrane protein, pIV; the inner membrane proteins, pI and pXI; and a cytoplasmic host factor, thioredoxin. Chemical cross-linking of intact cells demonstrates a trans-membrane complex containing pI and pIV. Formation of the complex protects pI from proteolytic cleavage by an endogenous protease. This protection also requires pXI, which is identical to the C-terminal portion of pI. This indicates that pXI, which is required for phage assembly in its own right, is also part of the complex. This complex forms in the absence of any other phage proteins or the DNA substrate; hence, it represents the first preinitiation step of phage morphogenesis. On the basis of protease protection data, we propose that the preinitiation complex is converted to an initiation complex by binding phage DNA, thioredoxin and the initiating minor coat protein(s).
Feng
J N
JN
The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Model
P
P
Russel
M
M
D001435:Bacteriophages / Q000187:drug effects / Q000502:physiology*; D001665:Binding Sites; D002213:Capsid / Q000235:genetics / Q000502:physiology*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism / Q000494:pharmacology; D017361:Viral Nonstructural Proteins / Q000235:genetics / Q000378:metabolism; D019065:Virus Assembly / Q000187:drug effects
D003432:Cross-Linking Reagents; D017361:Viral Nonstructural Proteins; C119520:pIV protein, Enterobacteria phage f1; D010450:Endopeptidases