Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin

Zhixiang Hu, Khadijeh Haghjoo, Frank Jordan

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Abstract

Evidence is presented for some secondary structure, very likely α- helical, of the propeptide of subtilisin E in aqueous salt solution, as well as for strong intermolecular interactions between the propeptide and the mature sequence both in the processed and unprocessed states (i.e. in prosubtilisin). Prosubtilisin is shown to exist as a dimer according to size exclusion high performance liquid chromatography under nondenaturing conditions; that dimer may be on the autoprocessing pathway. According to such a model, the prosequence of one prosubtilisin molecule is the template for the refolding of the mature sequence of the second, and, in turn, the hydrolytic process is intermolecular as well. Support for such an intermolecular folding model also includes potent slow binding inhibition of subtilisin by the propeptide, specific proteolysis of the propeptide by subtilisin, and evidence for intermolecular processing under a variety of conditions.

Original languageEnglish (US)
Pages (from-to)3375-3384
Number of pages10
JournalJournal of Biological Chemistry
Volume271
Issue number7
DOIs
StatePublished - Feb 16 1996

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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