کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5914118 | 1162720 | 2013 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Chaplins of Streptomyces coelicolor self-assemble into two distinct functional amyloids
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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چکیده انگلیسی
Chaplins are small, secreted proteins of streptomycetes that play instrumental roles in the formation of aerial hyphae and attachment of hyphae to surfaces. Here we show that the purified proteins self-assemble at a water/air interface into an asymmetric and amphipathic protein membrane that has an amyloid nature. Cryo-tomography reveals that the hydrophilic surface is relatively smooth, while the hydrophobic side is highly structured and characterized by the presence of small fibrils, which are similar to those observed on the surfaces of aerial hyphae. Interestingly, our work also provides evidence that chaplins in solution assemble into amyloid fibrils with a distinct morphology. These hydrophilic fibrils strongly resemble the structures known to be involved in attachment of Streptomyces hyphae to surfaces. These data for the first time show the assembly of bacterial proteins into two distinct amyloid structures that have different and relevant functions in vivo.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 184, Issue 2, November 2013, Pages 301-309
Journal: Journal of Structural Biology - Volume 184, Issue 2, November 2013, Pages 301-309
نویسندگان
Marcel Bokhove, Dennis Claessen, Wouter de Jong, Lubbert Dijkhuizen, Egbert J. Boekema, Gert T. Oostergetel,