کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1980523 1061863 2012 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
XPB helicase regulates DNA incision by the Thermoplasma acidophilum endonuclease Bax1
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
XPB helicase regulates DNA incision by the Thermoplasma acidophilum endonuclease Bax1
چکیده انگلیسی

Bax1 has recently been identified as a novel binding partner for the archaeal helicase XPB. We previously characterized Bax1 from Thermoplasma acidophilum as a Mg2+-dependent structure-specific endonuclease. Here we directly compare the endonuclease activity of Bax1 alone or in combination with XPB. Using several biochemical and biophysical approaches, we demonstrate regulation of Bax1 endonuclease activity by XPB. Interestingly, incision assays with Bax1 and XPB/Bax1 clearly demonstrate that Bax1 produces different incision patterns depending on the presence or absence of XPB. Using atomic force microscopy (AFM), we directly visualize and compare binding of Bax1 and XPB/Bax1 to different DNA substrates. Our AFM data support enhanced DNA binding affinity of Bax1 in the presence of XPB. Taken together, the DNA incision and binding results suggest that XPB is able to load and position Bax1 on the scissile DNA substrate, thus increasing the DNA substrate range of Bax1.


► Protein interaction controlled endonuclease regulation.
► Functions of nucleotide excision repair proteins in archaea.
► Analysis of XPB/Bax1 complexes with DNA at the level of individual molecules using atomic force microscopy.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 11, Issue 3, 1 March 2012, Pages 286–293
نویسندگان
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