The Taf14 YEATS domain is a reader of histone crotonylation

The discovery of new histone modifications is unfolding at startling rates, however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associa...

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Autores principales: Andrews, Forest H., Shinsky, Stephen A., Shanle, Erin K., Bridgers, Joseph B., Gest, Anneliese, Tsun, Ian K., Krajewski, Krzysztof, Shi, Xiaobing, Strahl, Brian D., Kutateladze, Tatiana G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4871749/
https://www.ncbi.nlm.nih.gov/pubmed/27089029
http://dx.doi.org/10.1038/nchembio.2065
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author Andrews, Forest H.
Shinsky, Stephen A.
Shanle, Erin K.
Bridgers, Joseph B.
Gest, Anneliese
Tsun, Ian K.
Krajewski, Krzysztof
Shi, Xiaobing
Strahl, Brian D.
Kutateladze, Tatiana G.
author_facet Andrews, Forest H.
Shinsky, Stephen A.
Shanle, Erin K.
Bridgers, Joseph B.
Gest, Anneliese
Tsun, Ian K.
Krajewski, Krzysztof
Shi, Xiaobing
Strahl, Brian D.
Kutateladze, Tatiana G.
author_sort Andrews, Forest H.
collection PubMed
description The discovery of new histone modifications is unfolding at startling rates, however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity.
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spelling pubmed-48717492016-10-18 The Taf14 YEATS domain is a reader of histone crotonylation Andrews, Forest H. Shinsky, Stephen A. Shanle, Erin K. Bridgers, Joseph B. Gest, Anneliese Tsun, Ian K. Krajewski, Krzysztof Shi, Xiaobing Strahl, Brian D. Kutateladze, Tatiana G. Nat Chem Biol Article The discovery of new histone modifications is unfolding at startling rates, however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine binding activity. 2016-04-18 2016-06 /pmc/articles/PMC4871749/ /pubmed/27089029 http://dx.doi.org/10.1038/nchembio.2065 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Andrews, Forest H.
Shinsky, Stephen A.
Shanle, Erin K.
Bridgers, Joseph B.
Gest, Anneliese
Tsun, Ian K.
Krajewski, Krzysztof
Shi, Xiaobing
Strahl, Brian D.
Kutateladze, Tatiana G.
The Taf14 YEATS domain is a reader of histone crotonylation
title The Taf14 YEATS domain is a reader of histone crotonylation
title_full The Taf14 YEATS domain is a reader of histone crotonylation
title_fullStr The Taf14 YEATS domain is a reader of histone crotonylation
title_full_unstemmed The Taf14 YEATS domain is a reader of histone crotonylation
title_short The Taf14 YEATS domain is a reader of histone crotonylation
title_sort taf14 yeats domain is a reader of histone crotonylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4871749/
https://www.ncbi.nlm.nih.gov/pubmed/27089029
http://dx.doi.org/10.1038/nchembio.2065
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