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

Fingerprint

Retroelements
Capsid Proteins
Virion
Yeasts
Cryoelectron Microscopy
Capsid
Particle Size
Proteins

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

Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein. / Al-Khayat, Hind A.; Bhella, David; Kenney, John M.; Roth, Jeanne Françoise; Kingsman, Alan J.; Martin-Rendon, Enca; Saibil, Helen R.

In: Journal of Molecular Biology, Vol. 292, No. 1, 10.09.1999, p. 65-73.

Research output: Contribution to journalArticle

Al-Khayat, HA, Bhella, D, Kenney, JM, Roth, JF, Kingsman, AJ, Martin-Rendon, E & Saibil, HR 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, vol. 292, no. 1, pp. 65-73. https://doi.org/10.1006/jmbi.1999.3055
Al-Khayat, Hind A. ; Bhella, David ; Kenney, John M. ; Roth, Jeanne Françoise ; Kingsman, Alan J. ; Martin-Rendon, Enca ; Saibil, Helen R. / Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein. In: Journal of Molecular Biology. 1999 ; Vol. 292, No. 1. pp. 65-73.
@article{06125ea232cb4b6da2096ddc4be33d95,
title = "Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein",
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.",
keywords = "Cryo-electron microscopy, Icosahedral 3D reconstruction, Ty retrotransposon, Virus-like particles",
author = "Al-Khayat, {Hind A.} and David Bhella and Kenney, {John M.} and Roth, {Jeanne Fran{\cc}oise} and Kingsman, {Alan J.} and Enca Martin-Rendon and Saibil, {Helen R.}",
year = "1999",
month = "9",
day = "10",
doi = "10.1006/jmbi.1999.3055",
language = "English",
volume = "292",
pages = "65--73",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein

AU - Al-Khayat, Hind A.

AU - Bhella, David

AU - Kenney, John M.

AU - Roth, Jeanne Françoise

AU - Kingsman, Alan J.

AU - Martin-Rendon, Enca

AU - Saibil, Helen R.

PY - 1999/9/10

Y1 - 1999/9/10

N2 - 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.

AB - 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.

KW - Cryo-electron microscopy

KW - Icosahedral 3D reconstruction

KW - Ty retrotransposon

KW - Virus-like particles

UR - http://www.scopus.com/inward/record.url?scp=0033543555&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033543555&partnerID=8YFLogxK

U2 - 10.1006/jmbi.1999.3055

DO - 10.1006/jmbi.1999.3055

M3 - Article

VL - 292

SP - 65

EP - 73

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -