Premium
Symmetry, flexibility and permeability in the structure of yeast retrotransposon virus‐like particles.
Author(s) -
Burns N.R.,
Saibil H.R.,
White N.S.,
Pardon J.F.,
Timmins P.A.,
Richardson S.M.,
Richards B.M.,
Adams S.E.,
Kingsman S.M.,
Kingsman A.J.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05156.x
Subject(s) - white (mutation) , library science , biology , computer science , genetics , gene
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.