Capsid flexibility during Ty1 virus-like particle assembly.

ABSTRACT: The Ty1/Copia family (Pseudoviridae) is a widely studied group of long terminal repeat (LTR) retrotransposons present in diverse eukaryotes that share a common ancestor with retroviruses. The founding member Ty1 of Saccharomyces assembles into heterogeneous virus-like particles (VLPs) that are composed of the Gag and Gag-Pol proteins. We used cryo-electron tomography (cryo-ET) of Ty1 VLPs purified from a Ty1-less yeast strain expressing a functional Ty1 element to determine the organization and interactions of Gag in Ty1 VLPs. Using sub-tomogram averaging (STA), we observed unique capsomere structures and obtained EM density maps for pentagonal (7.5 Å) and hexagonal (7.9 Å) capsomeres. Through iterative rounds of alignment and classification, we demonstrate that Ty1 VLPs are

SUBMITTER: Sibert BS 

PROVIDER: S-EPMC12724554 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature