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Biochem Biophys Res Commun. 1996 Dec 13;229(2):381-7.

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

Author information

1
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, Korea.

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.

PMID:
8954908
DOI:
10.1006/bbrc.1996.1814
[Indexed for MEDLINE]

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