Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein

Hind A. Al-Khayat, David Bhella, John M. Kenney, Jeanne Françoise Roth, Alan J. Kingsman, Enca Martin-Rendon, Helen R. Saibil

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The virus-like particles (VLPs) produced by the yeast Ty retrotransposons are structurally and functionally related to retroviral cores. Using cryo-electron microscopy (cryo-EM) and three-dimensional (3D) reconstruction, we have examined the structures of VLPs assembled from full-length and truncated forms of the capsid structural protein. The VLPs are highly polydisperse in their radius distribution. We have found that the length of the C-terminal region of the capsid structural protein dictates the T-number, and thus the size, of the assembled particles. Each construct studied appears to assemble into at least two or three size classes, with shorter C termini giving rise to smaller particles. This assembly property provides a model for understanding the variable assembly of retroviral core proteins. The particles are assembled from trimer-clustered units and there are holes in the capsid shells.

Original languageEnglish
Pages (from-to)65-73
Number of pages9
JournalJournal of Molecular Biology
Volume292
Issue number1
DOIs
Publication statusPublished - 10 Sep 1999
Externally publishedYes

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Keywords

  • Cryo-electron microscopy
  • Icosahedral 3D reconstruction
  • Ty retrotransposon
  • Virus-like particles

ASJC Scopus subject areas

  • Virology

Cite this

Al-Khayat, H. A., Bhella, D., Kenney, J. M., Roth, J. F., Kingsman, A. J., Martin-Rendon, E., & Saibil, H. R. (1999). Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein. Journal of Molecular Biology, 292(1), 65-73. https://doi.org/10.1006/jmbi.1999.3055