PXD042390

PXD042390 is an original dataset announced via ProteomeXchange.

Title	Testing the effect of histone native chemical ligation on protein binding to di-nucleosomes
Description	Here we examined whether histones H3 and H4 produced using native chemical ligation reaction affect protein binding to di-nucleosomes. To test this we performed a set of affinity purification pull-downs using di-nucleosomes containing the following histones H3 and H4: 1. unmodified ligated histone H3 and recombinant wild type histone H4 (unmod. H3), 2. recombinant wild type histone H3 and ligated unmodified histone H4 (unmod. H4) 3. ligated unmodified histones H3 and H4 (unmod. H3&H4). 4. recombinant wild type histones H3 and H4 (WT) Each pull-down was performed in three replicates. Co-purified proteins were quantified using label-free MS. Note that ligated histones H3 and H4 contain T32C or I29C single amino acid substitutions, respectively, that are introduced by the native chemical ligation procedure. In addition, ligated histone H4 is N-terminally acetylated to mimic its naturally blocked N-terminus.
HostingRepository	PRIDE
AnnounceDate	2024-04-29
AnnouncementXML	Submission_2024-04-29_08:03:01.427.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andrey Tvardovskiy
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-05-22 03:17:59	ID requested
1	2023-12-12 16:03:53	announced
⏵ 2	2024-04-29 08:03:02	announced	2024-04-29: Updated project metadata.

Lukauskas S, Tvardovskiy A, Nguyen NV, Stadler M, Faull P, Ravnsborg T, Ö, zdemir Aygenli B, Dornauer S, Flynn H, Lindeboom RGH, Barth TK, Brockers K, Hauck SM, Vermeulen M, Snijders AP, M, ü, ller CL, DiMaggio PA, Jensen ON, Schneider R, Bartke T, Decoding chromatin states by proteomic profiling of nucleosome readers. Nature, 627(8004):671-679(2024) [pubmed]

10.1038/s41586-024-07141-5;

submitter keyword: nucleosome pull-down,native chemical ligation

Till Bartke
contact affiliation	Institute of Functional Epigenetics, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
contact email	till.bartke@helmholtz-muenchen.de
lab head
Andrey Tvardovskiy
contact affiliation	Institute of Functional Epigenetics, Helmholtz Zentrum München, 85764 Neuherberg, Germany
contact email	tvardovsky.a@gmail.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/12/PXD042390

PRIDE project URI

• PRIDE
  1. PXD042390
     1. Label: PRIDE project
     2. Name: Testing the effect of histone native chemical ligation on protein binding to di-nucleosomes