Two-hybrid analysis of Ty3 capsid subdomain interactions

• Main Authors: Zhang Min, Larsen Liza SZ, Irwin Becky, Bilanchone Virginia, Sandmeyer Suzanne
• Format: Article
• Language: English
• Published: BMC 2010-05-01
• Series: Mobile DNA
• Online Access: http://www.mobilednajournal.com/content/1/1/14

<p>Abstract</p> <p>Background</p> <p>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.</p> <p>Findings</p> <p>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.</p> <p>Conclusions</p> <p>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.</p>