کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10824047 | 1061965 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Base excision repair in nucleosomes lacking histone tails
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کلمات کلیدی
APEBERXRCC1AP EndonucleaseUDGWRNDNA polymerase β - DNA پلیمراز بUracil DNA glycosylase - DNA گلیکوزیلاز اوراسیلbase excision repair - تعمیر پایه پایهbase pair - جفت پایهNucleotide - نوکلئوتیدnucleosome core particle - هسته هسته هسته ایWerner syndrome protein - پروتئین سندرم ورنرpol β - پل بChromatin - کروماتینGlycosylase - گلیکوزیلاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Recently, we developed an in vitro system using human uracil DNA glycosylase (UDG), AP endonuclease (APE), DNA polymerase β (pol β) and rotationally positioned DNA containing a single uracil associated with a 'designed' nucleosome, to test short-patch base excision repair (BER) in chromatin. We found that UDG and APE carry out their catalytic activities with reduced efficiency on nucleosome substrates, showing a distinction between uracil facing 'out' or 'in' from the histone surface, while DNA polymerase β (pol β) is completely inhibited by nucleosome formation. In this report, we tested the inhibition of BER enzymes by the N-terminal 'tails' of core histones that take part in both inter- and intra-nucleosome interactions, and contain sites of post-translational modifications. Histone tails were removed by limited trypsin digestion of 'donor' nucleosome core particles and histone octamers were exchanged onto a nucleosome-positioning DNA sequence containing a single G:U mismatch. The data indicate that UDG and APE activities are not significantly enhanced with tailless nucleosomes, and the distinction between rotational settings of uracil on the histone surface is unaffected. More importantly, the inhibition of pol β activity is not relieved by removal of the histone tails, even though these tails interact with DNA in the G:U mismatch region. Finally, inclusion of X-ray cross complement group protein 1 (XRCC1) or Werner syndrome protein (WRN) had no effect on the BER reactions. Thus, additional activities may be required in cells for efficient BER of at least some structural domains in chromatin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 4, Issue 2, 3 February 2005, Pages 203-209
Journal: DNA Repair - Volume 4, Issue 2, 3 February 2005, Pages 203-209
نویسندگان
Brian C. Beard, Jill J. Stevenson, Samuel H. Wilson, Michael J. Smerdon,