Identification and Analysis of Six Phosphorylation Sites Within the Xenopus laevis Linker Histone H1.0 C-Terminal Domain Indicate Distinct Effects on Nucleosome Structure.

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作者： Fanfan,Hao ^[1] ; Laxmi N,Mishra ^[1] ; Prasoon,Jaya ^[2] ; Richard,Jones ^[3] ; Jeffrey J,Hayes ^[4]

作者单位： Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, USA. ^[1] Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, USA; Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA. ^[2] MS Bioworks, Ann Arbor, Michigan, USA. ^[3] Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, USA. Electronic address: jeffrey_hayes@urmc.rochester.edu. ^[4]

关键词 FRET H1 C-terminal domain H1 CTD condensation H1 phosphorylation H1 phosphorylation affects nucleosome structure linker DNA trajectory linker histone mass spectrometry nucleosome reconstitution nucleosome structure

主题词动物(Animals);染色质(Chromatin);DNA(DNA);组蛋白类(Histones);核小体(Nucleosomes);磷酰化(Phosphorylation);光滑爪蟾(Xenopus laevis)

DOI 10.1016/j.mcpro.2022.100250

PMID 35618225

发布时间 2022-08-16

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