کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8323395 | 1539891 | 2014 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biophysical characterization of sites of host adaptive mutation in the influenza A virus RNA polymerase PB2 RNA-binding domain
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کلمات کلیدی
FAMHEKATCCRdRpRlucfluorescein amiditenuclear magnetic resonance - رزونانس مغناطیسی هستهایFLuc - FLUCRNA-dependent RNA polymerase - RNA پلیمراز وابسته به RNAelectrophoretic mobility shift assays - آزمایشات تحرک تحرک الکتروفورزNMR - تشدید مغناطیسی هستهای renilla luciferase - رگیلا لوسیفرازEMSA یا electrophoretic mobility shift assay - سنجش تغییر تحرک الکتروفورتیکFirefly luciferase - لوسیفراز فیرفیلیAmerican Type Culture Collection - مجموعه فرهنگی نوع آمریکاییhuman embryonic kidney - کلیه جنین انسان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Biophysical characterization of sites of host adaptive mutation in the influenza A virus RNA polymerase PB2 RNA-binding domain Biophysical characterization of sites of host adaptive mutation in the influenza A virus RNA polymerase PB2 RNA-binding domain](/preview/png/8323395.png)
چکیده انگلیسی
Influenza RNA polymerase is composed of three subunits, PA, PB1, and PB2, which interact with each other for transcription and replication of the viral RNA genome in the nucleus of infected cells. PB2 RNA-binding 627-domain (residues 535-693), located in the C-terminus, presents a highly basic surface around residue lysine 627 and has been proposed to interact with viral or cellular factors, resulting in host adaptation. However, the function of this domain is not yet characterized in detail. In this study, we identified RNA-binding activity and RNA-binding surfaces in both the N-terminal and basic C-terminal regions of PB2 627-domain using NMR experiments. Through mutagenesis studies, we confirmed which residues directly interact with RNA and mapped their locations on the RNA-binding surface. In addition, by luciferase activity assays, we showed that influenza virus polymerase activity may correlate with the interaction between PB2 and RNA. Representative host adaptive mutations (residues 591 and 627) were found to be located on the RNA-binding surface and were confirmed to directly interact with RNA and to affect polymerase activity. From these results, we suggest that influenza virus polymerase activity may be regulated through the interaction between PB2 627-domain and RNA and that consequently host adaptation of the virus may be influenced.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 53, August 2014, Pages 237-245
Journal: The International Journal of Biochemistry & Cell Biology - Volume 53, August 2014, Pages 237-245
نویسندگان
Kyungeun Lim, Meehyein Kim, Mi-Kyung Lee, Junsang Ko, Sungwoo Hong, Byong-Seok Choi,