PXD032292

PXD032292 is an original dataset announced via ProteomeXchange.

Title	Identification and analysis of phosphorylation within Xenopus laevis linker histone H1.0
Description	As a key structural component of the chromatin of higher eukaryotes, linker histones (H1s) are involved in stabilizing the folding of extended nucleosome arrays into higher-order chromatin structures and function as a gene-specific regulators of transcription in vivo. The H1 C-terminal domain (CTD) is essential for high affinity binding of linker histones to chromatin and stabilization of higher-order chromatin structure. Importantly, the H1 CTD is an intrinsically disordered domain that undergoes a drastic condensation upon binding to nucleosomes. Moroever, although phosphorylation is a prevalent posttranslational modification (PTM) within the H1 CTD, exactly where this modification is installed and how phosphorylation influences the structure of the H1 CTD remains unclear for many H1s. Using novel mass spectrometry techniques, we identified six phosphorylation sites within the CTD of the archetypal linker histone Xenopus H1.0. We then analyzed nucleosome-dependent CTD condensation and H1-dependent linker DNA conformation for six full-length H1s in which the phosphorylated serine residues were replaced by glutamic acid residues.
HostingRepository	PRIDE
AnnounceDate	2022-08-12
AnnouncementXML	Submission_2022-08-11_23:46:21.806.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD032292
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Jeffrey Hayes
SpeciesList	scientific name: Xenopus laevis (African clawed frog); NCBI TaxID: 8355;
ModificationList	phosphorylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-03-15 03:32:16	ID requested
⏵ 1	2022-08-11 23:46:22	announced

Hao F, Mishra LN, Jaya P, Jones R, Hayes JJ, Identification and Analysis of Six Phosphorylation Sites Within the Xenopus laevis Linker Histone H1.0 C-Terminal Domain Indicate Distinct Effects on Nucleosome Structure. Mol Cell Proteomics, 21(7):100250(2022) [pubmed]

submitter keyword: Identification and analysis of phosphorylation within Xenopus laevis linker histone H1.0

Jeffrey J. Hayes, Ph.D.
contact affiliation	Shohei Koide Professor and Chair, Department of Biochemistry and Biophysics Box 712, Rm 3-6710 University of Rochester Medical Center 601 Elmwood Ave Rochester, NY 14642
contact email	jeffrey_hayes@urmc.rochester.edu
lab head
Jeffrey Hayes
contact affiliation	University of Rochester
contact email	Jeffrey_Hayes@URMC.Rochester.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD032292
     1. Label: PRIDE project
     2. Name: Identification and analysis of phosphorylation within Xenopus laevis linker histone H1.0