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Two-hybrid analysis of Ty3 capsid subdomain interactions

BACKGROUND: The yeast retrotransposon Ty3 forms stable virus-like particles. Gag3, the major structural protein, is composed of capsid, spacer and nucleocapsid domains. The capsid domain of Gag3 was previously modeled as a structure similar to retrovirus capsid. FINDINGS: Two-hybrid analysis was use...

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Detalles Bibliográficos
Autores principales: Zhang, Min, Larsen, Liza SZ, Irwin, Becky, Bilanchone, Virginia, Sandmeyer, Suzanne
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878294/
https://www.ncbi.nlm.nih.gov/pubmed/20444245
http://dx.doi.org/10.1186/1759-8753-1-14
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author Zhang, Min
Larsen, Liza SZ
Irwin, Becky
Bilanchone, Virginia
Sandmeyer, Suzanne
author_facet Zhang, Min
Larsen, Liza SZ
Irwin, Becky
Bilanchone, Virginia
Sandmeyer, Suzanne
author_sort Zhang, Min
collection PubMed
description BACKGROUND: The yeast retrotransposon Ty3 forms stable virus-like particles. Gag3, the major structural protein, is composed of capsid, spacer and nucleocapsid domains. The capsid domain of Gag3 was previously modeled as a structure similar to retrovirus capsid. FINDINGS: Two-hybrid analysis was used to understand the interactions that contribute to particle assembly. Gag3 interacted with itself as predicted based on its role as the major structural protein. The N-terminal subdomain (NTD) of the capsid was able to interact with itself and with the C-terminal subdomain (CTD) of the capsid, but interacted less well with intact Gag3. Mutations previously shown to block particle assembly disrupted Gag3 interactions more than subdomain interactions. CONCLUSIONS: The findings that the NTD interacts with itself and with the CTD are consistent with previous modeling and a role similar to that of the capsid in retrovirus particle structure. These results are consistent with a model in which the Gag3-Gag3 interactions that initiate assembly differ from the subdomain interactions that potentially underlie particle stability.
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spelling pubmed-28782942010-05-29 Two-hybrid analysis of Ty3 capsid subdomain interactions Zhang, Min Larsen, Liza SZ Irwin, Becky Bilanchone, Virginia Sandmeyer, Suzanne Mob DNA Short Report BACKGROUND: The yeast retrotransposon Ty3 forms stable virus-like particles. Gag3, the major structural protein, is composed of capsid, spacer and nucleocapsid domains. The capsid domain of Gag3 was previously modeled as a structure similar to retrovirus capsid. FINDINGS: Two-hybrid analysis was used to understand the interactions that contribute to particle assembly. Gag3 interacted with itself as predicted based on its role as the major structural protein. The N-terminal subdomain (NTD) of the capsid was able to interact with itself and with the C-terminal subdomain (CTD) of the capsid, but interacted less well with intact Gag3. Mutations previously shown to block particle assembly disrupted Gag3 interactions more than subdomain interactions. CONCLUSIONS: The findings that the NTD interacts with itself and with the CTD are consistent with previous modeling and a role similar to that of the capsid in retrovirus particle structure. These results are consistent with a model in which the Gag3-Gag3 interactions that initiate assembly differ from the subdomain interactions that potentially underlie particle stability. BioMed Central 2010-05-05 /pmc/articles/PMC2878294/ /pubmed/20444245 http://dx.doi.org/10.1186/1759-8753-1-14 Text en Copyright ©2010 Zhang et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Report
Zhang, Min
Larsen, Liza SZ
Irwin, Becky
Bilanchone, Virginia
Sandmeyer, Suzanne
Two-hybrid analysis of Ty3 capsid subdomain interactions
title Two-hybrid analysis of Ty3 capsid subdomain interactions
title_full Two-hybrid analysis of Ty3 capsid subdomain interactions
title_fullStr Two-hybrid analysis of Ty3 capsid subdomain interactions
title_full_unstemmed Two-hybrid analysis of Ty3 capsid subdomain interactions
title_short Two-hybrid analysis of Ty3 capsid subdomain interactions
title_sort two-hybrid analysis of ty3 capsid subdomain interactions
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878294/
https://www.ncbi.nlm.nih.gov/pubmed/20444245
http://dx.doi.org/10.1186/1759-8753-1-14
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