کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914413 | 1570448 | 2012 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif
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کلمات کلیدی
ABCCTDNBDABC ATPaseElectrophoretic mobility shift assay - آزمون تحرک تحرک الکتروفورزNMR - تشدید مغناطیسی هستهای C-terminal domain - دامنه C ترمینالnucleotide-binding domain - دامنه اتصال دهنده نوکلئوتیدیEMSA یا electrophoretic mobility shift assay - سنجش تغییر تحرک الکتروفورتیکCoiled coil - کویل کویل شدهATP-binding cassette - کیت اتصال به ATP
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The bacterial Uup protein belongs to the REG subfamily of soluble ATP-binding cassette (ABC) ATPases, and is implicated in precise excision of transposons. In Escherichia coli, the uup gene encodes a 72 kDa polypeptide that comprises two ABC domains, separated by a linker region, and a 12 kDa C-terminal domain (CTD). Uup binds double-stranded DNA with no sequence specificity, and we previously demonstrated that the CTD domain is a crucial region that participates in DNA-binding activity. We report herein the NMR structure of Uup CTD, consisting of an intramolecular antiparallel two-stranded coiled coil motif. Structural comparison with analogous coiled coil domains reveals that Uup CTD contains an atypical 310-helix in the α-hairpin region that contributes to the hydrophobic core. Using NMR titration experiments, we identified residues of the CTD domain involved in the binding to double-stranded DNA. These residues are located on two opposite surfaces at the base of the coiled coil, formed by the N- and C-terminal extremities, where a strictly conserved proline residue induces an overwinding of the coiled coil. Finally, preliminary analysis of NMR spectra recorded on distinct Uup constructs precludes a fully flexible positioning of the CTD domain in full-length Uup. These structural data are the first reported for a non-ATPase domain within ABC REG subfamily.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 180, Issue 3, December 2012, Pages 577-584
Journal: Journal of Structural Biology - Volume 180, Issue 3, December 2012, Pages 577-584
نویسندگان
Ludovic Carlier, A. Sander Haase, Monica Y. Burgos Zepeda, Elie Dassa, Olivier Lequin,