Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

FEBS Lett. 1986 Jan 6;194(2):253-7. doi: 10.1016/0014-5793(86)80095-3.

Abstract

Here we demonstrate significant similarities between the amino acid sequences of trypsin (a serine protease) and the N-terminal piece of a specific fragment of the poliovirus polyprotein encompassing the sequence of the viral proteinase 3C, and also between cathepsin H (a cysteine protease) and the C-terminal piece of the same fragment. A coherent alignment of the sequences of the 3 proteases was obtained, in which the principal catalytically active residues occupy identical positions. A hypothesis is proposed that the viral enzyme may provide an evolutionary link between serine and cysteine protease families.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Evolution
  • Cathepsin H
  • Cathepsins / genetics
  • Cattle
  • Cysteine Endopeptidases
  • DNA-Directed RNA Polymerases / genetics
  • Endopeptidases / genetics*
  • Poliovirus / enzymology
  • Poliovirus / genetics*
  • RNA, Viral / analysis
  • Rats
  • Serine Endopeptidases
  • Trypsin / genetics

Substances

  • RNA, Viral
  • DNA-Directed RNA Polymerases
  • Cathepsins
  • Endopeptidases
  • Serine Endopeptidases
  • Trypsin
  • Cysteine Endopeptidases
  • Cathepsin H
  • Ctsh protein, rat