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Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones
Author(s) -
Takagi Hiroshi,
Koga Mihoko,
Katsurada Saori,
Yabuta Yukihiro,
Shinde Ujwal,
Inouye Masayori,
Nakamori Shigeru
Publication year - 2001
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/s0014-5793(01)03053-8
Subject(s) - subtilisin , protein precursor , proteases , chemistry , biochemistry , protease , protein folding , biology , enzyme
Several proteases require propeptides for the correct folding of their own protease domain. We have recently found that the propeptide from a thermostable subtilisin homolog aqualysin I can refold subtilisin BPN′ when added in trans . Here, we constructed chimeric genes with subtilisin E and aqualysin I to attempt the in cis folding of subtilisin E by means of the propeptide of aqualysin I. Our results indicate that the propeptide of aqualysin I can to some extent chaperone the intramolecular folding of the denatured subtilisin E. These results suggest that propeptides in the subtilisin family, despite their sequence diversity, have similar functions. Further, some enzymatic properties of some chimeras in which the subtilisin mature domain is partly swapped with that of aqualysin I were shown to be more similar to those of aqualysin I.