کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10823342 | 1061826 | 2013 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions
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کلمات کلیدی
BEROligodeoxynucleotidesS. pombeAP EndonucleaseAPE19–1–1MYH-associated polyposisEtBrODNHSQCSchizosaccharomyces pombeS. cerevisiaeGSTMEFIDC7,8-dihydro-8-oxoguanine - 7،8-دی هیدرو-8-اکسوگوئینapurinic/apyrimidinic - apurinic / apyrimidinicBSA - BSADNA glycosylase - DNA گلیکوزیلازbovine serum albumin - آلبومین سرم گاوethidium bromide - اتیدیوم برومایدHuman - انسانbase excision repair - تعمیر پایه پایهSaccharomyces cerevisiae - ساکارومایسس سرویزیهmouse embryonic fibroblast - موش فیبروبلاست جنینیmap - نقشهglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions](/preview/png/10823342.png)
چکیده انگلیسی
MutY homologue (MYH) is a DNA glycosylase which excises adenine paired with the oxidative lesion 7,8-dihydro-8-oxoguanine (8-oxoG, or Go) during base excision repair (BER). Base excision by MYH results in an apurinic/apyrimidinic (AP) site in the DNA where the DNA sugar-phosphate backbone remains intact. A key feature of MYH activity is its physical interaction and coordination with AP endonuclease I (APE1), which subsequently nicks DNA 5â² to the AP site. Because AP sites are mutagenic and cytotoxic, they must be processed by APE1 immediately after the action of MYH glycosylase. Our recent reports show that the interdomain connector (IDC) of human MYH (hMYH) maintains interactions with hAPE1 and the human checkpoint clamp Rad9-Rad1-Hus1 (9-1-1) complex. In this study, we used NMR chemical shift perturbation experiments to determine hMYH-binding site on hAPE1. Chemical shift perturbations indicate that the hMYH IDC peptide binds to the DNA-binding site of hAPE1 and an additional site which is distal to the APE1 DNA-binding interface. In these two binding sites, N212 and Q137 of hAPE1 are key mediators of the MYH/APE1 interaction. Intriguingly, despite the fact that hHus1 and hAPE1 both interact with the MYH IDC, hHus1 does not compete with hAPE1 for binding to hMYH. Rather, hHus1 stabilizes the hMYH/hAPE1 complex both in vitro and in cells. This is consistent with a common theme in BER, namely that the assembly of protein-DNA complexes enhances repair by efficiently coordinating multiple enzymatic steps while simultaneously minimizing the release of harmful repair intermediates.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 12, Issue 12, December 2013, Pages 1043-1052
Journal: DNA Repair - Volume 12, Issue 12, December 2013, Pages 1043-1052
نویسندگان
Paz J. Luncsford, Brittney A. Manvilla, Dimeka N. Patterson, Shuja S. Malik, Jin Jin, Bor-Jang Hwang, Randall Gunther, Snigdha Kalvakolanu, Leonora J. Lipinski, Weirong Yuan, Wuyuan Lu, Alexander C. Drohat, A.-Lien Lu, Eric A. Toth,