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Title: Protein Kinase A-mediated Serine 35 Phosphorylation Dissociates Histone H1.4 from Mitotic Chromosome.
Authors: Chi-Shuen Chu;Pang-Hung Hsu;Pei-Wen Lo;Elisabeth Scheer;Laszlo Tora;Hang-Jen Tsai;Ming-Daw Tsai;Li-Jung Juan
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2011
Issue Date: 2018-03-26T06:46:34Z
Publisher: The Journal of Biological Chemistry
Abstract: Abstract: Global histone H1 phosphorylation correlates with cell cycle progression. However, the function of site-specific H1 variant phosphorylation remains unclear. Our mass spectrometry analysis revealed a novel N-terminal phosphorylation of the major H1 variant H1.4 at serine 35 (H1.4S35ph), which accumulates at mitosis immediately after H3 phosphorylation at serine 10. Protein kinase A (PKA) was found to be a kinase for H1.4S35. Importantly, Ser-35-phosphorylated H1.4 dissociates from mitotic chromatin. Moreover, H1.4S35A substitution mutant cannot efficiently rescue the mitotic defect following H1.4 depletion, and inhibition of PKA activity increases the mitotic chromatin compaction depending on H1.4. Our results not only indicate that PKA-mediated H1.4S35 phosphorylation dissociates H1.4 from mitotic chromatin but also suggest that this phosphorylation is necessary for specific mitotic functions.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45555
Appears in Collections:[Department of Life Science] Periodical Articles

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