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

AL-Khayat, H.A., Bhella, D. , Kenney, J.M., Roth, J.F., Kingsman, A.J., Martin-Rendon, E. and 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), pp. 65-73. (doi:10.1006/jmbi.1999.3055)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Bhella, Dr David
Authors: AL-Khayat, H.A., Bhella, D., Kenney, J.M., Roth, J.F., Kingsman, A.J., Martin-Rendon, E., and Saibil, H.R.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Journal of Molecular Biology
Publisher:Academic Press
ISSN:0022-2836

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