Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein1 Export

@article{citeulike:6067437, 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.}, author = {AL-Khayat, Hind A. and Bhella, David and Kenney, John M. and Roth, Jeanne-Fran\c{c}oise and Kingsman, Alan J. and Martin-Rendon, Enca and Saibil, Helen R.}, citeulike-article-id = {6067437}, citeulike-linkout-0 = {http://dx.doi.org/10.1006/jmbi.1999.3055}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0022283699930553}, day = {10}, doi = {10.1006/jmbi.1999.3055}, issn = {00222836}, journal = {Journal of Molecular Biology}, keywords = {3d\_reconstruction, capsid, electron\_microscopy, erv, ty\_virus, yeast}, month = {September}, number = {1}, pages = {65--73}, posted-at = {2009-11-04 11:57:20}, priority = {2}, title = {Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein1}, url = {http://dx.doi.org/10.1006/jmbi.1999.3055}, volume = {292}, year = {1999} }

TY - JOUR ID - citeulike:6067437 L3 - citeulike-article-id:6067437 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. IS - 1 JF - Journal of Molecular Biology SN - 00222836 EP - 73 TI - Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein1 VL - 292 SP - 65 KW - 3d_reconstruction KW - capsid KW - electron_microscopy KW - erv KW - ty_virus KW - yeast AU - AL-Khayat, Hind AU - Bhella, David AU - Kenney, John AU - Roth, Jeanne-Françoise AU - Kingsman, Alan AU - Martin-Rendon, Enca AU - Saibil, Helen PY - 1999/09/10/ UR - http://dx.doi.org/10.1006/jmbi.1999.3055 ER -