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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Beckett D,Uhlenbeck OCdoi
10.1016/0022-2836(88)90052-6subject
Has Abstractpub_date
1988-12-20 00:00:00pages
927-38issue
4eissn
0022-2836issn
1089-8638pii
0022-2836(88)90052-6journal_volume
204pub_type
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