PXD040685

PXD040685 is an original dataset announced via ProteomeXchange.

Title	An unexpected histone-binding activity for the MIER1 histone deacetylase complex suggests a potential chaperone function.
Description	Histone deacetylases 1 and 2 (HDAC1/2) serve as the catalytic subunit of six distinct families of nuclear complexes. These complexes repress gene transcription through removing acetyl groups from lysine residues in histone tails. In addition to the deacetylase subunit, these complexes typically contain transcription factor and/or chromatin binding activities. The MIER:HDAC complex has hitherto been poorly characterized. Here we show that MIER1 unexpectedly co-purifies with an H2A:H2B histone dimer. We show that MIER1 is also able to bind a complete histone octamer. Intriguingly, we found that a larger MIER1:HDAC1:BAHD1:C1QBP complex additionally co-purifies with an intact nucleosome on which H3K27 is either di- or tri-methylated. Together this suggests that the MIER1 complex acts downstream of PRC2 to expand regions of repressed chromatin and could potentially deposit histone octamer onto nucleosome-depleted regions of DNA.
HostingRepository	PRIDE
AnnounceDate	2023-04-14
AnnouncementXML	Submission_2023-04-14_07:05:05.593.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	MarkCollins
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monomethylated residue; acetylated residue; monohydroxylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2023-03-08 03:50:59	ID requested
⏵ 1	2023-04-14 07:05:05	announced

Dataset with its publication pending

submitter keyword: methylation, deacetylase,Histone

MarkCollins
contact affiliation	School of Biosciences, University of Sheffield.
contact email	mark.collins@sheffield.ac.uk
lab head
MarkCollins
contact affiliation	University of Sheffield
contact email	mark.collins@sheffield.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD040685
     1. Label: PRIDE project
     2. Name: An unexpected histone-binding activity for the MIER1 histone deacetylase complex suggests a potential chaperone function.