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5HT - Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3

ABSTRACT: we provide evidence for a new class of histone posttranslational modification (PTM): serotonylation.

OTHER RELATED OMICS DATASETS IN: GSE117910

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: henrik molina

LAB HEAD: Ian Maze

PROVIDER: PXD008106 | Pride | 2018-12-19

REPOSITORIES: Pride

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Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.

Farrelly Lorna A LA Thompson Robert E RE Zhao Shuai S Lepack Ashley E AE Lyu Yang Y Bhanu Natarajan V NV Zhang Baichao B Loh Yong-Hwee E YE Ramakrishnan Aarthi A Vadodaria Krishna C KC Heard Kelly J KJ Erikson Galina G Nakadai Tomoyoshi T Bastle Ryan M RM Lukasak Bradley J BJ Zebroski Henry H Alenina Natalia N Bader Michael M Berton Olivier O Roeder Robert G RG Molina Henrik H Gage Fred H FH Shen Li L Garcia Benjamin A BA Li Haitao H Muir Tom W TW Maze Ian I

Nature 20190313 7749

Chemical modifications of histones can mediate diverse DNA-templated processes, including gene transcription<sup>1-3</sup>. Here we provide evidence for a class of histone post-translational modification, serotonylation of glutamine, which occurs at position 5 (Q5ser) on histone H3 in organisms that produce serotonin (also known as 5-hydroxytryptamine (5-HT)). We demonstrate that tissue transglutaminase 2 can serotonylate histone H3 tri-methylated lysine 4 (H3K4me3)-marked nucleosomes, resulting ...[more]

PMID: 30867594

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Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.

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