کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10765906 | 1050607 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Distinct recognition loop dynamics in cryptochrome-DASH and photolyase revealed by limited proteolysis
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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![عکس صفحه اول مقاله: Distinct recognition loop dynamics in cryptochrome-DASH and photolyase revealed by limited proteolysis Distinct recognition loop dynamics in cryptochrome-DASH and photolyase revealed by limited proteolysis](/preview/png/10765906.png)
چکیده انگلیسی
Cryptochromes (CRY) are light-responsive flavoproteins that play central roles in nature and human health, including circadian rhythm regulation. They are closely related to photolyases (PL), but, unlike PL, they cannot repair cyclobutane pyrimidine dimers (CPD) or [6-4] photoproducts in duplex DNA. Yet, if the barrier for flipping the CPD from the duplex is reduced, CRY-DASH, the subclass most structurally homologous to CPD PL, binds and repairs CPD like PL. Here, using limited proteolysis, we have identified the most flexible loops in CPD PL. One corresponds to a “recognition loop” that changes conformation substantially during substrate binding, and engages key interactions with the flipped CPD and the complementary DNA strand. Proteolysis kinetics reveal that the homologous loop in CRY-DASH is at least 10-fold more reactive. We propose that heightened dynamics of the recognition loop in CRY-DASH contribute to its compromised DNA base flipping, and its evolution of divergent function from PL.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 385, Issue 3, 31 July 2009, Pages 424-429
Journal: Biochemical and Biophysical Research Communications - Volume 385, Issue 3, 31 July 2009, Pages 424-429
نویسندگان
Neahlanna R. Mcleod, Matthew A. Brolich, Michael J. Damiani, Melanie A. O'Neill,