کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10822791 | 1061708 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A cradle for new proteins: trigger factor at the ribosome
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During ongoing synthesis, nascent protein chains are particularly sensitive to aggregation and degradation because they emerge from the ribosome in an unfolded state. In bacteria, the first protein to interact with nascent chains and facilitate their folding is the ribosome-associated chaperone trigger factor. Recently, crystal structures of trigger factor and of its ribosome-binding domain in complex with the large ribosomal subunit revealed that the chaperone adopts an extended 'dragon-shaped' fold with a large hydrophobic cradle, which arches over the exit of the ribosomal tunnel and shields newly synthesized proteins. These structural results, together with recent biochemical data on trigger factor and its interplay with other chaperones and factors that interact with the nascent chain, provide a comprehensive view of the role of trigger factor during co-translational protein folding.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Structural Biology - Volume 15, Issue 2, April 2005, Pages 204-212
Journal: Current Opinion in Structural Biology - Volume 15, Issue 2, April 2005, Pages 204-212
نویسندگان
Timm Maier, Lars Ferbitz, Elke Deuerling, Nenad Ban,