Dataset Information

Human Histone Sulfated Tyrosine Identification

ABSTRACT: Tyrosine sulfation is a common posttranslational modification in mammals. To date, it has been thought to be limited to secreted and transmembrane proteins, but little is known about tyrosine sulfation on nuclear proteins.To search for tyrosine sulfation on nuclear proteins, we purified the nucleus of HepG2 cells and searched for Ysulf using HPLC–MS/MS.We noted a peptide that is highly indicative of sulfation on the tyrosine 99 residue of histone H3(H3Y99sulf).We synthesized the peptides with the same primary sequence and modifications as were identified in the HPLC–MS/MS analysis: The synthesized H3Y99sulf peptides and their in vivo counterparts showed similar chromatographic and mass spectrum profiles in the same HPLC–MS/MS system . These results demonstrate that H3Y99sulf is an undocumented histone modification

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Cell Culture

DISEASE(S): Liver Cancer

SUBMITTER: Weixing Yu

LAB HEAD: Yugang Wang

PROVIDER: PXD043754 | Pride | 2023-07-13

REPOSITORIES: Pride

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Histone tyrosine sulfation by SULT1B1 regulates H4R3me2a and gene transcription.

Yu Weixing W Zhou Runxin R Li Nan N Lei Zhi-Chao ZC Guo Dingyuan D Peng Fei F Li Yan Y Bai Xue X Feng Shan S Wang Yu Y He Jie J Yin Sibi S Zeng Xiao X He Leya L Gao Yuan Y Li Mingchang M Guo Yusong R YR Liu Ke K Wang Yugang Y

Nature chemical biology 20230220 7

Tyrosine sulfation is a common posttranslational modification in mammals. To date, it has been thought to be limited to secreted and transmembrane proteins, but little is known about tyrosine sulfation on nuclear proteins. Here we report that SULT1B1 is a histone sulfotransferase that can sulfate the tyrosine 99 residue of nascent histone H3 in cytosol. The sulfated histone H3 can be transported into the nucleus and majorly deposited in the promoter regions of genes in chromatin. While the H3Y99 ...[more]

PMID: 36805701

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Project description:This model is described in the article: Kinetics of histone gene expression during early development of Xenopus laevis. Koster JG, Destrée OH and Westerhoff HV. J Theor Biol. 1988 Nov 21;135(2):139-67. PMID: 3267765 Abstract: Using literature data for transcriptional and translational rate constants, gene copy numbers, DNA concentrations, and stability constants, we have calculated the expected concentrations of histones and histone mRNA during embryogenesis of Xenopus laevis. The results led us to conclude that: (i) for X. laevis the gene copy number of the histone genes is too low to ensure the synthesis of sufficient histones during very early development, inheritance from the oocyte of either histone protein or histone mRNA (but not necessarily both) is necessary; (ii) from the known storage of histones in the oocyte and the rates of histone synthesis determined by Adamson and Woodland (1977), there would be sufficient histones to structure the newly synthesized DNA up to gastrulation but not thereafter (these empirical rates of histone synthesis may be underestimates); (iii) on the other hand, the amount of H3 mRNA recently observed during early embryogenesis (Koster, 1987, Koster et al., 1988) could direct a higher and sufficient synthesis of H3 protein, also after gastrulation. We present a quantitative model that accounts both for the observed H3 mRNA concentration as a function of time during embryogenesis and for the synthesis of sufficient histones to structure the DNA throughout early embryogenesis. The model suggests that X. laevis exhibits a major (i.e. some 14-fold) reduction in transcription of histone genes approximately 11 hours after fertilization. This reduction could be due to a decrease in the number of transcribed histone genes, a decreased rate constant of transcription with continued transcription of all the histone genes, and/or a reduction in the time during the cell cycle in which histone mRNA synthesis takes place. Alternatively, the histone mRNA stability might decrease approximately 16-fold 11 hours after fertilization. This model originates from BioModels Database: A Database of Annotated Published Models. It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not.. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

			Action	DRS
	ExtendedDataFig5b.lcd	Other
	ExtendedFig2g.msf	Msf
	ExtendedFig2g.raw	Raw
	HepG2_NUCLEUS_Fig1abc.raw	Raw
	LC-MS_of_H3Y99phospho-peptide.jpg	Other