کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10823355 | 1061826 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin
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کلمات کلیدی
NEILSpiroiminodihydantoinMCsBERFPGUDGNthEndonuclease III2,6-diamino-4-hydroxy-5-formamidopyrimidine - 2،6-دیامینو-4-هیدروکسی-5-فرمامیدوپیریمیدینapurinic/apyrimidinic - apurinic / apyrimidinicDNA glycosylase - DNA گلیکوزیلازUracil DNA glycosylase - DNA گلیکوزیلاز اوراسیلROS - ROSDNA damage - آسیبDNAOxidation - اکسیداسیونbase excision repair - تعمیر پایه پایهsingle-stranded - تک رشتهNEI - درdouble-stranded - دو رشتهmultiple cloning site - سایت کلونینگ چندگانهcolumn volume - ستون حجمFapy - فایپGuanidinohydantoin - گوانیدین هیداناتینReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Base excision repair is the major pathway for removal of oxidative DNA base damage. This pathway is initiated by DNA glycosylases, which recognize and excise damaged bases from DNA. In this work, we have purified the glycosylase domain (GD) of human DNA glycosylase NEIL3. The substrate specificity has been characterized and we have elucidated the catalytic mechanisms. GD NEIL3 excised the hydantoin lesions spiroiminodihydantoin (Sp) and guanidinohydantoin (Gh) in single-stranded (ss) and double-stranded (ds) DNA efficiently. NEIL3 also removed 5-hydroxy-2â²-deoxycytidine (5OHC) and 5-hydroxy-2â²-deoxyuridine (5OHU) in ssDNA, but less efficiently than hydantoins. Unlike NEIL1 and NEIL2, which possess a β,δ-elimination activity, NEIL3 mainly incised damaged DNA by β-elimination. Further, the base excision and strand incision activities of NEIL3 exhibited a non-concerted action, indicating that NEIL3 mainly operate as a monofunctional DNA glycosylase. The site-specific NEIL3 mutant V2P, however, showed a concerted action, suggesting that the N-terminal amino group in Val2 is critical for the monofunctional modus. Finally, we demonstrated that residue Lys81 is essential for catalysis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 12, Issue 12, December 2013, Pages 1159-1164
Journal: DNA Repair - Volume 12, Issue 12, December 2013, Pages 1159-1164
نویسندگان
Silje Z. Krokeide, Jon K. Laerdahl, Medya Salah, Luisa Luna, F. Henning Cederkvist, Aaron M. Fleming, Cynthia J. Burrows, Bjørn Dalhus, Magnar Bjørås,