کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10757366 | 1050394 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
ATP binding to two sites is necessary for dimerization of nucleotide-binding domains of ABC proteins
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کلمات کلیدی
ABCNBSNBDLRETABC transporter - ABC حمل کنندهLuminescence resonance energy transfer - انتقال انرژی تابشی لومینسانسDimerization - اندازه گیریnucleotide-binding domain - دامنه اتصال دهنده نوکلئوتیدیnucleotide-binding site - سایت پیوند نوکلئوتیدیKinetics - سینتیک (جنبش شناسی) Fluorescence - فلورسنسATP-binding cassette - کیت اتصال به ATP
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
ATP binding cassette (ABC) transporters have a functional unit formed by two transmembrane domains and two nucleotide binding domains (NBDs). ATP-bound NBDs dimerize in a head-to-tail arrangement, with two nucleotides sandwiched at the dimer interface. Both NBDs contribute residues to each of the two nucleotide-binding sites (NBSs) in the dimer. In previous studies, we showed that the prototypical NBD MJ0796 from Methanocaldococcus jannaschii forms ATP-bound dimers that dissociate completely following hydrolysis of one of the two bound ATP molecules. Since hydrolysis of ATP at one NBS is sufficient to drive dimer dissociation, it is unclear why all ABC proteins contain two NBSs. Here, we used luminescence resonance energy transfer (LRET) to study ATP-induced formation of NBD homodimers containing two NBSs competent for ATP binding, and NBD heterodimers with one active NBS and one binding-defective NBS. The results showed that binding of two ATP molecules is necessary for NBD dimerization. We conclude that ATP hydrolysis at one nucleotide-binding site drives NBD dissociation, but two binding sites are required to form the ATP-sandwich NBD dimer necessary for hydrolysis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 1, 3 January 2014, Pages 97-102
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 1, 3 January 2014, Pages 97-102
نویسندگان
Maria E. Zoghbi, Guillermo A. Altenberg,