کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882361 | 1536555 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cys redox reactions and metal binding of a Cys2His2 zinc finger
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Cys redox reactions and metal binding of a Cys2His2 zinc finger Cys redox reactions and metal binding of a Cys2His2 zinc finger](/preview/png/9882361.png)
چکیده انگلیسی
The elucidation of mechanisms by which cysteine (Cys) redox reactions influence metal binding to zinc finger domains is important for understanding the structure and function of zinc fingers. The present studies utilize electrospray ionization mass spectrometry (ESI-MS) to analyze Cys redox reactions and their influence on metal ion binding to a synthetic polypeptide similar in motif to the third zinc finger of the RNA polymerase II transcription factor, Sp1 (Sp1-3). The differential specificity of metal binding events to this zinc finger domain is demonstrated over a range of redox-altering dithiothreitol, hydrogen peroxide, and hydrogen ion concentrations. By analyzing this Cys2His2 zinc finger domain at single Da resolution with ESI-MS, shifts in the natural isotope cluster demonstrate that a Cys thiol and thiolate can contribute to Zn2+ and other metal ion coordination. These experiments provide insight into the basic redox chemistry and metal binding mechanisms of Cys2His2 zinc finger domains.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 434, Issue 1, 1 February 2005, Pages 139-149
Journal: Archives of Biochemistry and Biophysics - Volume 434, Issue 1, 1 February 2005, Pages 139-149
نویسندگان
Jason L. Larabee, James R. Hocker, Jay S. Hanas,