Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action

In view of the cationic amphipathic structure of tachyplesin I and antiparallel beta-sheet as a general DNA binding motif, DNA binding of the antimicrobial peptide has been examined. Several footprinting-like techniques using DNase I protection, dimethyl sulfate protection, and bleomycin- (BLM-) ind...

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Bibliographic Details
Published in:Biochemistry (Easton) 1992-03, Vol.31 (11), p.2998-3004
Main Authors: Yonezawa, Atsuo, Kuwahara, Jun, Fujii, Nobutaka, Sugiura, Yukio
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anti-Infective Agents - chemistry
Anti-Infective Agents - metabolism
Antibacterial agents
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antimicrobial Cationic Peptides
Base Sequence
Binding Sites
Biological and medical sciences
Bleomycin - pharmacology
Circular Dichroism
Deoxyribonuclease I
Dithiothreitol - pharmacology
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins
Medical sciences
Molecular Sequence Data
Peptides - chemistry
Peptides - metabolism
Peptides, Cyclic
Pharmacology. Drug treatments
Protein Conformation
Structure-Activity Relationship
Sulfuric Acid Esters
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Summary:In view of the cationic amphipathic structure of tachyplesin I and antiparallel beta-sheet as a general DNA binding motif, DNA binding of the antimicrobial peptide has been examined. Several footprinting-like techniques using DNase I protection, dimethyl sulfate protection, and bleomycin- (BLM-) induced DNA cleavage were applied in this study. Some distinct footprints with DNase I are detected, and also the sequence-specific cleavage mode of the BLM-Fe(II) complex clearly is altered in the presence of tachyplesin I. In addition, methylation of the N-7 residue of guanine situated in the DNA major groove is not entirely inhibited (or activated) by tachyplesin I. The results suggest that tachyplesin I interacts with the minor groove of DNA duplex. Disappearance of the footprints by dithiothreitol-treated tachyplesin I and Ala-tachyplesin strongly suggests a significant contribution of secondary structure containing an antiparallel beta-sheet to the DNA binding of tachyplesin I. This is the first report on DNA interaction with a small peptide which contains a unique antiparallel beta-sheet structure. The mechanism for antimicrobial action of tachyplesin I has also been inferred.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00126a022