کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10755596 | 1050376 | 2014 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans
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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
چکیده انگلیسی
RNA binding proteins control gene expression by the attenuation/antitermination mechanism. HutP is an RNA binding antitermination protein. It regulates the expression of hut operon when it binds with RNA by modulating the secondary structure of single-stranded hut mRNA. HutP necessitates the presence of l-histidine and divalent metal ion to bind with RNA. Herein, we report the crystal structures of ternary complex (HutP-l-histidine-Mg2+) and EDTA (0.5Â M) treated ternary complex (HutP-l-histidine-Mg2+), solved at 1.9Â Ã
and 2.5Â Ã
resolutions, respectively, from Geobacillus thermodenitrificans. The addition of 0.5Â M EDTA does not affect the overall metal-ion mediated ternary complex structure and however, the metal ions at the non-specific binding sites are chelated, as evidenced from the results of structural features.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 945-951
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 945-951
نویسندگان
Viswanathan Thiruselvam, Padavattan Sivaraman, Thirumananseri Kumarevel, Mondikalipudur Nanjappagounder Ponnuswamy,