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. 1992 Mar;11(3):1155–1164. doi: 10.1002/j.1460-2075.1992.tb05156.x

Symmetry, flexibility and permeability in the structure of yeast retrotransposon virus-like particles.

N R Burns 1, H R Saibil 1, N S White 1, J F Pardon 1, P A Timmins 1, S M Richardson 1, B M Richards 1, S E Adams 1, S M Kingsman 1, A J Kingsman 1
PMCID: PMC556558  PMID: 1312462

Abstract

The virus-like particles (VLPs) of the yeast retrotransposon Ty are genetically, structurally and functionally analogous to retroviral nucleocapsids or cores. Like retroviral cores Ty-VLPs package and possibly promote the enzyme activities for reverse transcription and integration, as well as encapsulating the RNA that is the intermediate in retrotransposition. Here we show that Ty-VLPs assemble into symmetrical structures across a broad distribution of particle sizes. This spread of sizes violates the principle of quasi-equivalent packing. In addition, RNase accessibility experiments suggest that these particles form an open structure that does not protect the encapsulated RNA. These features distinguish Ty-VLPs from typical spherical viral capsids in both structure and function.

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