Evidence for propeptide-assisted folding of the calcium-dependent protease of the cyanobacterium Anabaena

Eur J Biochem. 1996 Nov 1;241(3):750-5. doi: 10.1111/j.1432-1033.1996.00750.x.

Abstract

The Ca(2+)-dependent protease of the cyanobacterium Anabaena variabilis is a cytoplasmic enzyme with a substrate specificity like trypsin. Its previously published DNA sequence [Maldener, I., Lockau, W., Cai, Y. & Wolk, C. P. (1991) Mol. Gen. Genet. 225, 113-120] contained a sequencing error. Here we report the corrected sequence which shows, that the Ca(2+)-protease belongs to the family of subtilases (subtilisin-like serine proteases). Consistent with its cytoplasmic localization, a pre-sequence is not found. The enzyme is produced as a precursor with a large amino-terminal propeptide. Expression of the pro-region and mature region (protease domain) in Escherichia coli cells in trans demonstrates that formation of the active enzyme requires the propeptide. The results demonstrate that propeptide-assisted protein folding also occurs with cytoplasmic enzymes, in support of the hypothesis that this mechanism is a widespread phenomenon.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anabaena / enzymology*
  • Anabaena / genetics
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Calcium / metabolism
  • Chromogenic Compounds
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Molecular Sequence Data
  • Protein Folding*
  • Protein Precursors / genetics
  • Protein Precursors / metabolism*
  • Recombinant Proteins / metabolism
  • Restriction Mapping
  • Sequence Analysis, DNA
  • Subtilisins / genetics
  • Subtilisins / metabolism*

Substances

  • Bacterial Proteins
  • Chromogenic Compounds
  • PrcA protein, bacteria
  • Protein Precursors
  • Recombinant Proteins
  • Subtilisins
  • Calcium

Associated data

  • GENBANK/X56955
  • GENBANK/X63439