Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: Daniel Panne
LAB HEAD: Daniel Panne
PROVIDER: PXD038798 | Pride | 2023-03-11
REPOSITORIES: Pride
Action | DRS | |||
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20210903_CoreNCP_1.raw | Raw | |||
20210903_CoreNCP_2.raw | Raw | |||
20210903_OnlyNCP_1.raw | Raw | |||
20210903_OnlyNCP_2.raw | Raw | |||
20210903_P300sNCP_1.raw | Raw |
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Ibrahim Ziad Z Wang Tao T Destaing Olivier O Salvi Nicola N Hoghoughi Naghmeh N Chabert Clovis C Rusu Alexandra A Gao Jinjun J Feletto Leonardo L Reynoird Nicolas N Schalch Thomas T Zhao Yingming Y Blackledge Martin M Khochbin Saadi S Panne Daniel D
Nature communications 20221215 1
Histone modifications are deposited by chromatin modifying enzymes and read out by proteins that recognize the modified state. BRD4-NUT is an oncogenic fusion protein of the acetyl lysine reader BRD4 that binds to the acetylase p300 and enables formation of long-range intra- and interchromosomal interactions. We here examine how acetylation reading and writing enable formation of such interactions. We show that NUT contains an acidic transcriptional activation domain that binds to the TAZ2 domai ...[more]