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The Ty virus-like particles (VLPs) are functionally analogous to retroviral particles. They package the enzymes and the RNA necessary for retrotransposition, and mediate the integration of the reverse-transcription product into the genome of the host cell. Here we map three structural determinants of particle assembly in the subunit protein. We have also identified key residues in these regions that seem to be involved in subunit interaction and particle morphology. In particular, two point mutations in putative amphipathic helices have remarkable effects on VLP morphology, increasing the diameter as much as eightfold.

Type

Journal article

Journal

Mol Microbiol

Publication Date

11/1996

Volume

22

Pages

667 - 679

Keywords

Amino Acid Sequence, DNA Transposable Elements, Gene Deletion, Molecular Sequence Data