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PMID: 9261411 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cryo-electron microscopy structure of yeast Ty retrotransposon virus-like particles.

Journal of virology ·Vol. 71 ·No. 9 ·1997-09-00 ·Pages 6863-8

Palmer KJ, Tichelaar W, Myers N, Burns NR, Butcher SJ, Kingsman AJ, Fuller SD, Saibil HR

Abstract

The virus-like particles (VLPs) produced by the yeast retrotransposon Ty1 are functionally related to retroviral cores. These particles are unusual in that they have variable radif. A paired mass-radius analysis of VLPs by scanning transmission electron microscopy showed that many of these particles form an icosahedral T-number series. Three-dimensional reconstruction to 38-A resolution from cryo-electron micrographs of T = 3 and T = 4 shells revealed that the single structural protein encoded by the TYA gene assembles into spiky shells from trimeric units.

MeSH Terms
Capsid/ultrastructure Cryopreservation DNA, Fungal/ultrastructure Microscopy, Electron Retroelements Retroviridae/ultrastructure Saccharomyces cerevisiae/genetics Virion
Chemicals
DNA, Fungal Retroelements
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Palmer K J
Department of Crystallography, Birkbeck College, London, United Kingdom.
Tichelaar W
Myers N
Burns N R
Butcher S J
Kingsman A J
Fuller S D
Saibil H R
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.71.9.6863-6868.1997
Published
1997-09-00
Pages
6863-8
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC191967
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.71.9.6863-6868.1997 PMC Full Text View journal details
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