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PXD053429-1

PXD053429 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleHistone monoaminylation dynamics are regulated by a single enzyme and promote neural rhythmicity
DescriptionHistone H3 monoaminylations at glutamine(Q) 5 represent an important family of epigenetic markers in neurons that play critical roles in the mediation of permissive gene expression (1, 2). We previously demonstrated that H3Q5 serotonylation(ser) and dopaminylation(dop) are catalyzed by the Transglutaminase 2 (TGM2) enzyme and alter both local and global chromatin states (3, 4). Here, we found that TGM2 additionally functions as an “eraser” of H3 monoaminylations that is capable of “rewriting” these epigenetic marks in cells, including a new class of this modification, H3Q5 histaminylation(his), which displays dynamic diurnal expression in brain and contributes to neural rhythmicity. We found that H3Q5his inhibits binding of the MLL1 complex to the H3 N-terminus and attenuates its methyltransferase activity on H3 lysine(K) 4. We determined that H3Q5 monoaminylation dynamics are dictated by local monoamine concentrations, which are utilized by TGM2. Taken together, we present here a novel mechanism through which a single chromatin regulatory enzyme is capable of sensing chemical microenvironments to affect the epigenetic states of cells.
HostingRepositoryPRIDE
AnnounceDate2024-10-11
AnnouncementXMLSubmission_2024-10-11_05:08:09.701.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterStephanie Stransky
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListNo PTMs are included in the dataset
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-06-26 07:25:49ID requested
12024-10-11 05:08:10announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: TGM2, serotonylation, neural rhythmicity,Histone H3
Contact List
Stephanie Stransky
contact affiliationDepartment of Biochemistry, Albert Einstein College of Medicine
contact emailstephanie.stransky@gmail.com
lab head
Stephanie Stransky
contact affiliationAlbert Einstein College of Medicine
contact emailstephanie.stransky@gmail.com
dataset submitter
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Dataset FTP location
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