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Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase
Author(s) -
Jia Yan,
Liu Hui,
Bao Wei,
Weng Meizhi,
Chen Wei,
Cai Yongjun,
Zheng Zhongliang,
Zou Guolin
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.11.011
Subject(s) - nattokinase , subtilisin , chaperone (clinical) , chemistry , protein precursor , protein folding , intramolecular force , in vivo , biochemistry , biology , stereochemistry , enzyme , medicine , microbiology and biotechnology , pathology , fermentation
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.