Abstract
The coat protein of the simple spherical (triangulation no. T = 3) RNA coliphage R17 protects the genomic RNA in the virus particle and acts as a translational repressor of the phage-encoded replicase gene. It has been suggested that these two functions are related and that the translational repression complex serves as a nucleation complex for subsequent assembly of the bacteriophage. We have used a translational operation fragment to examine the relationship between formation of the translational repression complex and the assembly of the protein into T = 3 capsids. In vitro analysis of the aggregation properties of R17 coat protein reveals that binding of the translational operator fragment to the protein dimer triggers polymerization of the protein into T = 3 capsids of well-defined composition. The data further implicate the translational operator in nucleation of assembly and suggest a possible physical-chemical basis of the nucleation step.
Original language | English (US) |
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Pages (from-to) | 927-938 |
Number of pages | 12 |
Journal | Journal of Molecular Biology |
Volume | 204 |
Issue number | 4 |
DOIs | |
State | Published - Dec 20 1988 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology