Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones

Hiroshi Takagi, Mihoko Koga, Saori Katsurada, Yukihiro Yabuta, Ujwal Shinde, Masayori Inouye, Shigeru Nakamori

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)210-214
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Nov 16 2001


  • Aqualysin I
  • Chimeric protease
  • Intramolecular chaperone
  • Propeptide
  • Protein folding
  • Subtilisin E

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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