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In vitroassembly of the outer shell of bacteriophage ϕ6 nucleocapsid

Authors
Journal
Virology
0042-6822
Publisher
Elsevier
Publication Date
Volume
166
Issue
1
Identifiers
DOI: 10.1016/0042-6822(88)90150-x
Disciplines
  • Biology

Abstract

Abstract Following dissociation of bacteriophage ϕ6 nucleocapsid (NC) by EDTA, a particle composed of protein P8 and corresponding to the outer shell of the NC was assembled in vitro in the presence of Ca 2+ and Mg 2+. Assembly was obtained from soluble protein constituents frove 100 μg/ml and was optimal within a temperature range of 22–30°. Assembly did not require the presence of genomic RNA. Crosslinking results of intact NCs and in vitro-assembled outer shells suggested that protein P8 dimers are the structural subunits of the shell. Analysis of the assembly kinetics by electron microscopy suggested that ring-like particles of uniform size, packed in flat hexagonal arrays, are intermediates in outer shell assembly.

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