کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048736 1074096 2010 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase
چکیده انگلیسی

Here, we show that during in vivo folding of the precursor, the propeptide of subtilisin nattokinase functions as an intramolecular chaperone (IMC) that organises the in vivo folding of the subtilisin domain. Two residues belonging to β-strands formed by conserved regions of the IMC are crucial for the folding of the subtilisin domain through direct interactions. An identical protease can fold into different conformations in vivo due to the action of a mutated IMC, resulting in different kinetic parameters. Some interfacial changes involving conserved regions, even those induced by the subtilisin domain, blocked subtilisin folding and altered its conformation. Insight into the interaction between the subtilisin and IMC domains is provided by a three-dimensional structural model.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 584, Issue 23, 1 December 2010, Pages 4789–4796
نویسندگان
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