Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control

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 minim...

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Autores principales:	Matthew A. Cottee, Sean L. Beckwith, Suzanne C. Letham, Sarah J. Kim, George R. Young, Jonathan P. Stoye, David J. Garfinkel, Ian A. Taylor
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/aae81f4107a84d3a99658b2407f95119
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spelling	oai:doaj.org-article:aae81f4107a84d3a99658b2407f951192021-12-02T18:14:23ZStructure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control10.1038/s41467-021-25849-02041-1723https://doaj.org/article/aae81f4107a84d3a99658b2407f951192021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25849-0https://doaj.org/toc/2041-1723In 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.Matthew A. CotteeSean L. BeckwithSuzanne C. LethamSarah J. KimGeorge R. YoungJonathan P. StoyeDavid J. GarfinkelIan A. TaylorNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Matthew A. Cottee Sean L. Beckwith Suzanne C. Letham Sarah J. Kim George R. Young Jonathan P. Stoye David J. Garfinkel Ian A. Taylor Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
description	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.
format	article
author	Matthew A. Cottee Sean L. Beckwith Suzanne C. Letham Sarah J. Kim George R. Young Jonathan P. Stoye David J. Garfinkel Ian A. Taylor
author_facet	Matthew A. Cottee Sean L. Beckwith Suzanne C. Letham Sarah J. Kim George R. Young Jonathan P. Stoye David J. Garfinkel Ian A. Taylor
author_sort	Matthew A. Cottee
title	Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
title_short	Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
title_full	Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
title_fullStr	Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
title_full_unstemmed	Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control
title_sort	structure of a ty1 restriction factor reveals the molecular basis of transposition copy number control
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/aae81f4107a84d3a99658b2407f95119
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Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control

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