Autor: |
Matthew A. Cottee, Sean L. Beckwith, Suzanne C. Letham, Sarah J. Kim, George R. Young, Jonathan P. Stoye, David J. Garfinkel, Ian A. Taylor |
Jazyk: |
angličtina |
Rok vydání: |
2021 |
Předmět: |
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Zdroj: |
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021) |
Druh dokumentu: |
article |
ISSN: |
2041-1723 |
DOI: |
10.1038/s41467-021-25849-0 |
Popis: |
In Saccharomyces cerevisiae, unchecked proliferation of Ty1 retrotransposons is controlled by the process of copy number control (CNC), which requires the p22/p18 protein, translated from an internal transcript within the Ty1 GAG gene. Here, the authors present the 2.8 Å crystal structure of a minimal p18 from Ty1-Gag that is able to restrict Ty1 transposition and identify two dimer interfaces in p18, whose roles were probed by mutagenesis both in vitro and in vivo. As p22/p18 contains only one of two conserved domains required for retroelement Gag assembly, they propose that p22/p18-Gag interactions block the Ty1 virus-like particle assembly pathway, resulting in defective particles incapable of supporting retrotransposition. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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