کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1927383 1536514 2006 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability
چکیده انگلیسی

To compare folding/assembly processes of heptameric co-chaperonin proteins 10 (cpn10) from different species and search for the origin of thermostability in hyper-thermostable Aquifex aeolicus cpn10 (Aacpn10), we have studied two bacterial variants—Aacpn10 and Escherichia coli cpn10 (GroES)—and compared the results to data on Homo sapiens cpn10 (hmcpn10). Equilibrium denaturation of GroES by urea, guanidine hydrochloride (GuHCl) and temperature results in coupled heptamer-to-monomer transitions in all cases. This is similar to the behavior of Aacpn10 but differs from hmcpn10 denaturation in urea. Time-resolved experiments reveal that GroES unfolds before heptamer dissociation, whereas refolding/reassembly begins with folding of individual monomers; these assemble in a slower step. The sequential folding/assembly mechanism for GroES is rather similar to that observed for Aacpn10 but contradicts the parallel paths of hmcpn10. We reveal that Aacpn10’s stability profile is shifted upwards, broadened, and also moved horizontally to higher temperatures, as compared to that of GroES.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 456, Issue 1, 1 December 2006, Pages 8–18
نویسندگان
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