کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9127133 | 1160201 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain
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کلمات کلیدی
GFPIPTGDTTIL-4ABLPP1NEB1,4-dithiothreitol - 1،4-dithiothreitolsodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدisopropyl β-D-thiogalactopyranoside - ایزوپروپیل β-D-thiogalactopyranosideProtein folding - تاشدگی پروتئینAggregation - تجمعpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازgreen fluorescent protein - پروتئین فلورسنت سبز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain](/preview/png/9127133.png)
چکیده انگلیسی
Green fluorescent protein (GFP) has been used to report protein folding by correlating solubility with fluorescence. In a GFP fusion protein, an upstream aggregation-prone domain can disrupt de novo folding of the GFP domain in Escherichia coli, resulting in a loss of fluorescence. Previously, we showed that prevention of misfolding of the upstream aggregation-prone domain by a coupled folding and binding interaction during protein synthesis restored both GFP fluorescence and solubility. Since molecular chaperones often fold nascent polypeptides through a bind-and-release interaction, the question remains whether the chaperone interaction with the upstream aggregation-prone domain enhances GFP fluorescence. Here, we demonstrate that a significant increase in GFP fluorescence occurred only when appropriate chaperones that recognized the aggregation-prone protein and helped its folding were co-expressed. A possible correlation between GFP fluorescence and the productive folding by chaperones is proposed. This study may provide a general strategy for identifying chaperones specific for difficult-to-fold proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 350, Issue 1, 25 April 2005, Pages 25-31
Journal: Gene - Volume 350, Issue 1, 25 April 2005, Pages 25-31
نویسندگان
Aihua Zhang, Eric J. Cantor, Tanya Barshevsky, Shaorong Chong,