کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882165 | 1536544 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interface mutation in heptameric co-chaperonin protein 10 destabilizes subunits but not interfaces
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
We here report on a human mitochondrial co-chaperonin protein 10 (cpn10) variant in which the conserved interface residue leucine-96 is replaced with glycine (Leu96Gly cpn10). According to analytical ultracentrifugation, the mutation does not perturb the ability to assemble into a heptamer and electron microscopy reveals that Leu96Gly cpn10 is ring-shaped like wild-type cpn10. Despite elimination of a hydrophobic residue, the subunit-subunit affinity is essentially identical in Leu96Gly cpn10 and in wild-type cpn10. This is explained by a compensating rearrangement in Leu96Gly cpn10, evident from cross-linking and gel-filtration experiments. As a direct result of lower monomer stability, Leu96Gly cpn10 is dramatically less stable towards chemical and thermal perturbations as compared to wild-type cpn10. We conclude that leucine-96 is an interface residue preserved to guarantee stable cpn10 monomers. Our study demonstrates that the cpn10 interfaces can adapt to structural alterations without loss of either subunit-subunit affinity or heptamer specificity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 439, Issue 2, 15 July 2005, Pages 175-183
Journal: Archives of Biochemistry and Biophysics - Volume 439, Issue 2, 15 July 2005, Pages 175-183
نویسندگان
Christopher Brown, Jue Liao, Pernilla Wittung-Stafshede,