کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1940644 1050785 2006 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Monoubiquitination of the nonhomologous end joining protein XRCC4
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Monoubiquitination of the nonhomologous end joining protein XRCC4
چکیده انگلیسی

Nonhomologous end joining is one of the major pathways by which cells repair double-strand breaks, and the XRCC4–DNA ligase IV complex is required for the ligation step. To better understand the regulation and stability of XRCC4 and DNA ligase IV, we investigated the ubiquitination status of these two proteins. We identified a predominantly monoubiquitinated form of XRCC4, and higher molecular weight forms of ubiquitinated XRCC4 were detected in lower abundance. In response to etoposide-induced DNA damage, ubiquitinated XRCC4 became more pronounced and was additionally phosphorylated. We confirmed that DNA ligase IV is unstable in the absence of XRCC4, with a half-life of approximately 30–90 min. Unlike XRCC4, we did not detect ubiquitinated forms of DNA ligase IV, and we found that the presence of XRCC4 stabilized DNA ligase IV more significantly than proteasome inhibitors. Monoubiquitination of XRCC4 may play a critical role in the regulation of nonhomologous end joining.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 341, Issue 1, 3 March 2006, Pages 175–183
نویسندگان
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