Proteomics

Dataset Information

0

Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding


ABSTRACT: Nuclear proteins bind chromatin to execute and regulate genome-templated processes. While structural and biochemical studies of individual nucleosome interactions have suggested that an acidic patch on the nucleosome disk surface may be a common site for recruitment to chromatin, the pervasiveness of acidic patch binding and whether other nucleosome surface binding hot-spots exist remains unclear. Here, we use nucleosome affinity proteomics with a library of nucleosomes that collectively disrupts all exposed histone surfaces to establish the universal principles of nucleosome binding. We find that the acidic patch and two adjacent surfaces are the primary hot-spots for nucleosome disk binding and are critical for the majority of nucleosome-protein interactions. In contrast, nearly half of the nucleosome disk surface participates only minimally in protein binding. In addition to establishing the fundamental principles of chromatin binding, our screen defines nucleosome surface requirements of nearly 300 nucleosome interacting proteins implicated in diverse nuclear processes including transcription, DNA damage repair, cell cycle regulation, and nuclear architecture. Building from our screen, we demonstrate that the Anaphase-Promoting Complex/Cyclosome directly binds the acidic patch and elucidate a redundant charge-based mechanism of acidic patch binding by nuclear pore protein ELYS. Overall, our interactome screen illuminates a highly competitive nucleosome binding hub for chromatin-targeted activities and curates a list of nucleosome interacting proteins that will enable mechanistic exploration of many unexpected chromatin-templated nuclear processes.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture, Embryonic Stem Cell

SUBMITTER: Dennis Goldfarb  

LAB HEAD: Robert McGinty

PROVIDER: PXD018690 | Pride | 2020-06-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MC007_nucleosome_TMT_WT_mut1_mut2.raw Raw
MC008_nucleosome_TMT_WT_mut3_mut4.raw Raw
MC009_nucleosome_TMT_WT_mut5_mut6.raw Raw
McGintyH2Mutants.fasta Fasta
Mouse_sp_2017-02-01.fasta Fasta
Items per page:
1 - 5 of 8

Similar Datasets

2023-02-14 | PXD032791 | Pride
2023-08-09 | GSE240192 | GEO
2019-06-11 | GSE121543 | GEO
2023-05-15 | GSE203073 | GEO
2015-08-21 | E-GEOD-65441 | biostudies-arrayexpress
2022-02-23 | PXD025287 | Pride
2021-02-10 | PXD020992 | Pride
2013-09-23 | E-GEOD-40064 | biostudies-arrayexpress
2013-09-23 | E-GEOD-40063 | biostudies-arrayexpress
2024-10-16 | PXD056554 | Pride