کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8325328 | 1539932 | 2011 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural and functional characterization of the N-terminal domain of human Rad51D
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کلمات کلیدی
HSQCBLMRAD51DNOESYEMSANuclear Overhauser Effect SpectroscopY - Spectroscopy اثر Overhauser هسته ایElectrophoretic mobility shift assay - آزمون تحرک تحرک الکتروفورزHolliday junction - اتصال HollidayNMR - تشدید مغناطیسی هستهای Protein–DNA interaction - تعامل پروتئین DNAStructure - ساختار یا سازهheteronuclear single quantum correlation spectroscopy - طیف سنجی همبستگی کوانتومی تک هسته ایHomologous recombination - نوترکیبی همولوگ
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural and functional characterization of the N-terminal domain of human Rad51D Structural and functional characterization of the N-terminal domain of human Rad51D](/preview/png/8325328.png)
چکیده انگلیسی
Rad51D, one of five Rad51 paralogs, is required for homologous recombination and disruption of Holliday junctions with bloom syndrome protein (BLM) in vertebrates. The N-terminal domain of Rad51D is highly conserved in eukaryotic Rad51D orthologs and is essential for protein-protein interaction with XRCC2, but nothing is known about its individual structure or function. In this study, we determined the solution structure of the human Rad51D N-terminal domain (residues 1-83), which consists of four short helices flanked by long N- and C-terminal tails. Interestingly, the position of the N-terminal tail (residues 1-13) is fixed within the domain structure via several hydrophobic interactions between Leu4 and Thr27, Leu4 and Val28, and Val6 and Ile17. We show that the domain preferentially binds to ssDNA versus dsDNA and does not bind to a mobile Holliday junction by electrophoretic mobility shift assay. NMR titration and dynamics studies showed that human Rad51D-N interacts with ssDNA by positively charged and hydrophobic residues on its surface. The results suggest that the N-terminal domain of Rad51D is required for the ssDNA-specific binding function of human Rad51D and that the conserved N-terminal domains of other Rad51 paralogs may have distinguishable functions from each other in homologous recombination.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 416-422
Journal: The International Journal of Biochemistry & Cell Biology - Volume 43, Issue 3, March 2011, Pages 416-422
نویسندگان
Young Mee Kim, Byong-Seok Choi,