Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4

The intrinsically disordered acidic activation domain (AD) of the yeast transcription factor Gal4 acts through binding to the Med15 subunit of the Mediator complex. Here, the authors show that Gal4 interacts with Med15 through an identical fuzzy binding mechanism as Gcn4 AD, which has a different se...

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Autores principales:	Lisa M. Tuttle, Derek Pacheco, Linda Warfield, Damien B. Wilburn, Steven Hahn, Rachel E. Klevit
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6edacede67b64527a4e957a257936932
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spelling	oai:doaj.org-article:6edacede67b64527a4e957a2579369322021-12-02T14:30:27ZMediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn410.1038/s41467-021-22441-42041-1723https://doaj.org/article/6edacede67b64527a4e957a2579369322021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22441-4https://doaj.org/toc/2041-1723The intrinsically disordered acidic activation domain (AD) of the yeast transcription factor Gal4 acts through binding to the Med15 subunit of the Mediator complex. Here, the authors show that Gal4 interacts with Med15 through an identical fuzzy binding mechanism as Gcn4 AD, which has a different sequence, revealing a common sequence-independent mechanism for AD-Mediator binding. In contrast, Gal4 AD binds to the Gal80 repressor as a structured polypeptide, which strongly suggests that the structured binding partner dictates the type of protein–protein interaction for an intrinsically disordered protein.Lisa M. TuttleDerek PachecoLinda WarfieldDamien B. WilburnSteven HahnRachel E. KlevitNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lisa M. Tuttle Derek Pacheco Linda Warfield Damien B. Wilburn Steven Hahn Rachel E. Klevit Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
description	The intrinsically disordered acidic activation domain (AD) of the yeast transcription factor Gal4 acts through binding to the Med15 subunit of the Mediator complex. Here, the authors show that Gal4 interacts with Med15 through an identical fuzzy binding mechanism as Gcn4 AD, which has a different sequence, revealing a common sequence-independent mechanism for AD-Mediator binding. In contrast, Gal4 AD binds to the Gal80 repressor as a structured polypeptide, which strongly suggests that the structured binding partner dictates the type of protein–protein interaction for an intrinsically disordered protein.
format	article
author	Lisa M. Tuttle Derek Pacheco Linda Warfield Damien B. Wilburn Steven Hahn Rachel E. Klevit
author_facet	Lisa M. Tuttle Derek Pacheco Linda Warfield Damien B. Wilburn Steven Hahn Rachel E. Klevit
author_sort	Lisa M. Tuttle
title	Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
title_short	Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
title_full	Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
title_fullStr	Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
title_full_unstemmed	Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4
title_sort	mediator subunit med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators gal4 and gcn4
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6edacede67b64527a4e957a257936932
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Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4

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