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  Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses

Dodonova, S. O., Prinz, S., Bilanchone, V., Sandmeyer, S., & Briggs, J. A. G. (2019). Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses. Proceedings of the National Academy of Sciences of the United States of America, 116(20), 10048-10057. doi:10.1073/pnas.1900931116.

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 Creators:
Dodonova, S. O., Author
Prinz, S., Author
Bilanchone, V., Author
Sandmeyer, S., Author
Briggs, John A. G.1, 2, Author           
Affiliations:
1European Molecular Biology Laboratory, External Organizations, ou_3346677              
2MRC Laboratory of Molecular Biology, External Organizations, Cambridge, GB, ou_3346673              

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Free keywords: LTR retrotransposon retrovirus capsid Gag maturation major homology region cryoelectron microscopy reverse-transcriptase terminal domain gag protein ty3 gag3 virus maturation particles element Science & Technology - Other Topics
 Abstract: Retroviruses evolved from long terminal repeat (LTR) retrotransposons by acquisition of envelope functions, and subsequently reinvaded host genomes. Together, endogenous retroviruses and LTR retrotransposons represent major components of animal, plant, and fungal genomes. Sequences from these elements have been exapted to perform essential host functions, including placental development, synaptic communication, and transcriptional regulation. They encode a Gag polypeptide, the capsid domains of which can oligomerize to form a virus-like particle. The structures of retroviral capsids have been extensively described. They assemble an immature viral particle through oligomerization of full-length Gag. Proteolytic cleavage of Gag results in amature, infectious particle. In contrast, the absence of structural data on LTR retrotransposon capsids hinders our understanding of their function and evolutionary relationships. Here, we report the capsid morphology and structure of the archetypal Gypsy retrotransposon Ty3. We performed electron tomography (ET) of immature and mature Ty3 particles within cells. We found that, in contrast to retroviruses, these do not change size or shape upon maturation. Cryo-ET and cryo-electron microscopy of purified, immature Ty3 particles revealed an irregular fullerene geometry previously described for mature retrovirus core particles and a tertiary and quaternary arrangement of the capsid (CA) C-terminal domain within the assembled capsid that is conserved with mature HIV-1. These findings provide a structural basis for studying retrotransposon capsids, including those domesticated in higher organisms. They suggest that assembly via a structurally distinct immature capsid is a later retroviral adaptation, while the structure of mature assembled capsids is conserved between LTR retrotransposons and retroviruses.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000467804000057
DOI: 10.1073/pnas.1900931116
ISSN: 0027-8424
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 116 (20) Sequence Number: - Start / End Page: 10048 - 10057 Identifier: -