cDNA cloning and characterization of buforin I, an antimicrobial peptide: a cleavage product of histone H2A

Biochem Biophys Res Commun. 1996 Dec 13;229(2):381-7. doi: 10.1006/bbrc.1996.1814.

Abstract

A cDNA containing coding information for buforin I, the toad stomach antimicrobial peptide, was identified by PCR. The cloned cDNA encoded a protein of 129 amino acids whose 39-amino-acid N-terminus was identical to buforin I. Nucleotide sequence analysis of the cloned cDNA revealed that it had over 90% amino acid homology with histone H2A, the replication-dependent protein. Both Northern and Southern blot analysis of the toad genome suggested that histone H2A and buforin I were encoded by the same gene. A specific protease responsible for the generation of buforin I from histone H2A was found to be present in the crude extracts of the toad stomach. These results suggest that there exists a specific regulation mechanism which converts the toad histone H2A to the antimicrobial peptide buforin I.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / metabolism*
  • Base Sequence
  • Blotting, Northern
  • Blotting, Southern
  • Bufonidae
  • Cloning, Molecular
  • DNA, Complementary
  • Gastric Mucosa / metabolism
  • Histones / metabolism*
  • Hydrolysis
  • Molecular Sequence Data
  • Peptides*
  • Proteins / genetics*
  • Proteins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Anti-Bacterial Agents
  • DNA, Complementary
  • Histones
  • Peptides
  • Proteins
  • buforin I

Associated data

  • GENBANK/U70133