کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10770562 | 1050834 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Functional interaction of Purα with the Cdk2 moiety of cyclin A/Cdk2
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Purα is a sequence-specific single-stranded nucleic acid-binding protein and a member of the highly conserved Pur family. Purα has been shown to colocalize with cyclin A/Cdk2 and to coimmunoprecipitate with cyclin A during S-phase. Here we show that this interaction is mediated by a specific affinity of Purα for Cdk2. In pull-down assays GST-Purα efficiently binds Cdk2 and Cdk1, binds Cdk4 less efficiently, and does not display binding to Cdk6. Purα stimulates several-fold the phosphorylation in vitro of histone H1 by cyclin A/Cdk2, produced from baculovirus constructs. Double chromatin immunoprecipitation using antibodies to Cdk2 and Purα reveals that both proteins colocalize in HeLa cells to DNA segments upstream of the c-MYC gene. Pur family member Purγ colocalizes with Cdk2 to a specific DNA segment in this region.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 4, 25 March 2005, Pages 851-857
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 4, 25 March 2005, Pages 851-857
نویسندگان
Hong Liu, Sharon M. Barr, Caryn Chu, D. Stave Kohtz, Yayoi Kinoshita, Edward M. Johnson,