کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10871930 | 1074092 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway](/preview/png/10871930.png)
چکیده انگلیسی
Phosphorylation of H2AX functions to recruit DNA repair complexes to sites of DNA damage. Here, we report that H2AX is constitutively acetylated on lysine 36 (H2AXK36Ac) by the CBP/p300 acetyltransferases. H2AXK36Ac is required for cells to survive exposure to ionizing radiation; however, H2AXK36Ac levels are not increased by DNA damage. Further, acetylation of H2AX did not affect phosphorylation of H2AX or the formation of DNA damage foci. Finally, cells with a double mutation in both the H2AX acetylation and phosphorylation sites were more radiosensitive than cells containing individual mutations. H2AXK36Ac is therefore a novel, constitutive histone modification located within the histone core region which regulates radiation sensitivity independently of H2AX phosphorylation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 584, Issue 13, 2 July 2010, Pages 2926-2930
Journal: FEBS Letters - Volume 584, Issue 13, 2 July 2010, Pages 2926-2930
نویسندگان
Xiaofeng Jiang, Ye Xu, Brendan D. Price,