Proteomics

Dataset Information

0

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): Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jason Low  

LAB HEAD: Joel Mackay

PROVIDER: PXD033633 | Pride | 2023-03-11

REPOSITORIES: Pride

altmetric image

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]

Similar Datasets

2014-01-16 | E-GEOD-52363 | biostudies-arrayexpress
2014-01-16 | E-GEOD-52419 | biostudies-arrayexpress
2021-06-17 | PXD022066 | Pride
2020-08-11 | PXD015231 | Pride
2015-06-27 | E-GEOD-70298 | biostudies-arrayexpress
2017-05-01 | GSE89675 | GEO
2020-12-07 | PXD017378 | Pride
2020-04-02 | PXD010370 | Pride
2023-05-08 | GSE229050 | GEO
2022-01-01 | GSE190369 | GEO