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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| Authors: | Fanfan Hao Laxmi N. Mishra Prasoon Jaya Richard Jones Jeffrey J. Hayes |
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| Affiliation: | 1. Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, USA;2. Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York, USA;3. MS Bioworks, Ann Arbor, Michigan, USA |
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| Abstract: | |
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| Keywords: | H1 C-terminal domain H1 phosphorylation H1 CTD condensation H1 phosphorylation affects nucleosome structure mass spectrometry FRET nucleosome reconstitution linker histone nucleosome structure linker DNA trajectory CDK" },{" #name" :" keyword" ," $" :{" id" :" kwrd0070" }," $$" :[{" #name" :" text" ," _" :" cyclin-dependent kinase CTD" },{" #name" :" keyword" ," $" :{" id" :" kwrd0080" }," $$" :[{" #name" :" text" ," _" :" C-terminal domain FDR" },{" #name" :" keyword" ," $" :{" id" :" kwrd0090" }," $$" :[{" #name" :" text" ," _" :" false discovery rate FRAP" },{" #name" :" keyword" ," $" :{" id" :" kwrd0100" }," $$" :[{" #name" :" text" ," _" :" fluorescence recovery after photobleaching GD" },{" #name" :" keyword" ," $" :{" id" :" kwrd0110" }," $$" :[{" #name" :" text" ," _" :" globular domain MS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0120" }," $$" :[{" #name" :" text" ," _" :" mass spectrometry MS/MS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0130" }," $$" :[{" #name" :" text" ," _" :" tandem mass spectrometry PTM" },{" #name" :" keyword" ," $" :{" id" :" kwrd0140" }," $$" :[{" #name" :" text" ," _" :" post-translational modification TE" },{" #name" :" keyword" ," $" :{" id" :" kwrd0150" }," $$" :[{" #name" :" text" ," _" :" Tris and EDTA |
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