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

1992; Springer Nature; Volume: 11; Issue: 3 Linguagem: Inglês

10.1002/j.1460-2075.1992.tb05156.x

1460-2075

Nigel R. Burns, Helen R. Saibil, Nicholas White, J. F. Pardon, Peter Timmins, Sarah M. Richardson, B. M. Richards, Sally E. Adams, Susan M. Kingsman, Alan J. Kingsman,

Fungal and yeast genetics research

Research Article1 March 1992free access Symmetry, flexibility and permeability in the structure of yeast retrotransposon virus-like particles. N.R. Burns N.R. Burns British Bio-technology Limited, Oxford, UK. Search for more papers by this author H.R. Saibil H.R. Saibil British Bio-technology Limited, Oxford, UK. Search for more papers by this author N.S. White N.S. White British Bio-technology Limited, Oxford, UK. Search for more papers by this author J.F. Pardon J.F. Pardon British Bio-technology Limited, Oxford, UK. Search for more papers by this author P.A. Timmins P.A. Timmins British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.M. Richardson S.M. Richardson British Bio-technology Limited, Oxford, UK. Search for more papers by this author B.M. Richards B.M. Richards British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.E. Adams S.E. Adams British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.M. Kingsman S.M. Kingsman British Bio-technology Limited, Oxford, UK. Search for more papers by this author A.J. Kingsman A.J. Kingsman British Bio-technology Limited, Oxford, UK. Search for more papers by this author N.R. Burns N.R. Burns British Bio-technology Limited, Oxford, UK. Search for more papers by this author H.R. Saibil H.R. Saibil British Bio-technology Limited, Oxford, UK. Search for more papers by this author N.S. White N.S. White British Bio-technology Limited, Oxford, UK. Search for more papers by this author J.F. Pardon J.F. Pardon British Bio-technology Limited, Oxford, UK. Search for more papers by this author P.A. Timmins P.A. Timmins British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.M. Richardson S.M. Richardson British Bio-technology Limited, Oxford, UK. Search for more papers by this author B.M. Richards B.M. Richards British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.E. Adams S.E. Adams British Bio-technology Limited, Oxford, UK. Search for more papers by this author S.M. Kingsman S.M. Kingsman British Bio-technology Limited, Oxford, UK. Search for more papers by this author A.J. Kingsman A.J. Kingsman British Bio-technology Limited, Oxford, UK. Search for more papers by this author Author Information N.R. Burns1, H.R. Saibil1, N.S. White1, J.F. Pardon1, P.A. Timmins1, S.M. Richardson1, B.M. Richards1, S.E. Adams1, S.M. Kingsman1 and A.J. Kingsman1 1British Bio-technology Limited, Oxford, UK. The EMBO Journal (1992)11:1155-1164https://doi.org/10.1002/j.1460-2075.1992.tb05156.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 11Issue 31 March 1992In this issue RelatedDetailsLoading ...