کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2184644 1095901 2014 15 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Context-Dependent Remodeling of Rad51–DNA Complexes by Srs2 Is Mediated by a Specific Protein–Protein Interaction
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
Context-Dependent Remodeling of Rad51–DNA Complexes by Srs2 Is Mediated by a Specific Protein–Protein Interaction
چکیده انگلیسی


• Rad51 bound on ssDNA is removed by the Srs2 helicase.
• Rad51 when bound on double-stranded DNA inhibits the DNA unwinding activity of the Srs2 helicase.
• Assembly of more than one Srs2 molecule on DNA is required for its unwinding activity.
• A physical interaction between Srs2 and Rad51 regulates DNA unwinding.

The yeast Srs2 helicase removes Rad51 nucleoprotein filaments from single-stranded DNA (ssDNA), preventing DNA strand invasion and exchange by homologous recombination. This activity requires a physical interaction between Srs2 and Rad51, which stimulates ATP turnover in the Rad51 nucleoprotein filament and causes dissociation of Rad51 from ssDNA. Srs2 also possesses a DNA unwinding activity and here we show that assembly of more than one Srs2 molecule on the 3′ ssDNA overhang is required to initiate DNA unwinding. When Rad51 is bound on the double-stranded DNA, its interaction with Srs2 blocks the helicase (DNA unwinding) activity of Srs2. Thus, in different DNA contexts, the physical interaction of Rad51 with Srs2 can either stimulate or inhibit the remodeling functions of Srs2, providing a means for tailoring DNA strand exchange activities to enhance the fidelity of recombination.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 426, Issue 9, 1 May 2014, Pages 1883–1897
نویسندگان
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