The involvement of two specific arginine residues in the action of HM-1 killer toxin was deduced from site-directed mutagenesis

Biol Pharm Bull. 2000 Aug;23(8):998-1000. doi: 10.1248/bpb.23.998.

Abstract

Each of the four arginine residues in the HM-1 killer toxin was replaced by alanine using site-directed mutagenesis. The polymerase chain reaction (PCR)-constructed mutant gene was successfully expressed in HM-1 toxin resistant Saccharomyces cerevisiae. Among four HM-1 toxin analogues, R82A HM-1 toxin and R86A HM-1 toxin lost killer activity, while R61A HM-1 toxin and R85A HM-1 toxin retained activity. These results strongly indicate the importance of the arginine residues at positions 82 and 86 which are located in the C-terminal region of the HM-1 toxin for the action of killer activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine / chemistry*
  • Base Sequence
  • DNA Primers
  • Killer Factors, Yeast
  • Mutagenesis, Site-Directed
  • Mycotoxins / chemistry
  • Mycotoxins / genetics
  • Mycotoxins / pharmacology*
  • Polymerase Chain Reaction

Substances

  • DNA Primers
  • Killer Factors, Yeast
  • Mycotoxins
  • Arginine