Proteomics

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The modulation of CHD4 nucleosome remodelling activity by auxiliary domains suggests unifies mechanistic aspects of chromatin remodelling across enzyme families

ABSTRACT: We determine the impact of auxiliary domains on the nucleosome sliding activity of CHD4. This dataset comprises the crosslinking mass spectrometry data we reported.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jason Low  

LAB HEAD: Joel Mackay

PROVIDER: PXD033633 | Pride | 2023-03-11

REPOSITORIES: Pride

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20201218_QEHFX3_JLow_JZ_XLMS_C1.raw Raw
20201218_QEHFX3_JLow_JZ_XLMS_C1_reinject.raw Raw
20201218_QEHFX3_JLow_JZ_XLMS_C2.raw Raw
20201218_QEHFX3_JLow_JZ_XLMS_C3.raw Raw
20201222_CHD4only_BS3_PLINK_SEARCH.zip Other
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Publications

The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families.

Zhong Yichen Y   Moghaddas Sani Hakimeh H   Paudel Bishnu P BP   Low Jason K K JKK   Silva Ana P G APG   Mueller Stefan S   Deshpande Chandrika C   Panjikar Santosh S   Reid Xavier J XJ   Bedward Max J MJ   van Oijen Antoine M AM   Mackay Joel P JP  

Nature communications 20221206 1

CHD4 is an essential, widely conserved ATP-dependent translocase that is also a broad tumour dependency. In common with other SF2-family chromatin remodelling enzymes, it alters chromatin accessibility by repositioning histone octamers. Besides the helicase and adjacent tandem chromodomains and PHD domains, CHD4 features 1000 residues of N- and C-terminal sequence with unknown structure and function. We demonstrate that these regions regulate CHD4 activity through different mechanisms. An N-term  ...[more]

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