کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8330009 | 1540239 | 2015 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Importance of a stable topoisomerase IB clamping for an efficient DNA processing: Effect of the Lys369Glu mutation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The role of lysine 369 of human topoisomerase IB in recognizing, clamping and processing its DNA substrate was experimentally investigated. Lys369 is located in one of the two lips that interact to each other allowing the protein to embrace and firmly bind the DNA substrate. The lysine was mutated to a glutamate residue and the catalytic activity of the mutant enzyme was assayed. The mutant shows a distributive behavior, has a reduced binding to the substrate and a lower cleavage extent when compared to the wild type enzyme. The mutant displays reduced sensitivity to CPT both “in vitro” and in an “in vivo” yeast model, likely because of the low amount of cleaved DNA, however it displays cleavage and religation rates comparable to the wild type. These results demonstrate that the mutation causes a destabilization of the lips clamping around the DNA, impairing the protein-DNA interaction, emphasizing the importance of the ionic pair in tuning the stability of the protein-DNA complex.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 81, November 2015, Pages 76-82
Journal: International Journal of Biological Macromolecules - Volume 81, November 2015, Pages 76-82
نویسندگان
Sara Vieira, Silvia Castelli, Alessandro Desideri,