Document Detail

Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T.
MedLine Citation:
PMID:  18706965     Owner:  NLM     Status:  MEDLINE    
Previous studies have led to the isolation of histone H2B with antibacterial properties from an extract of the skin of the Schlegel's green tree frog Rhacophorus schlegelii and it is now demonstrated that the intact peptide is released into norepinephrine-stimulated skin secretions. In order to investigate the mechanism of action of this peptide, a maltose-binding protein (MBP)-fused histone H2B (MBP-H2B) conjugate was prepared and subjected to antimicrobial assay. The fusion protein showed bacteriostatic activity against Escherichia coli strain JCM5491 with a minimum inhibitory concentration of 11 microM. The lysate prepared from JCM5491 cells was capable of fragmenting MBP-H2B within the histone H2B region, but the lysate from the outer membrane proteinase T (OmpT) gene-deleted BL21(DE3) cells was not. FITC-labeled MBP-H2B (FITC-MBP-H2B) penetrated into the bacterial cell membrane of JCM5491 and ompT-transformed BL21(DE3) cells, but not into ompT-deleted BL21(DE3) cells. Gel retardation assay using MBP-H2B-deletion mutants indicated that MBP-H2B bound to DNA at a site within the N-terminal region of histone H2B. Consequently, it is proposed that the antimicrobial action of histone H2B involves, at least in part, penetration of an OmpT-produced N-terminal histone H2B fragment into the bacterial cell membrane with subsequent inhibition of cell functions.
Hiroaki Kawasaki; Takumi Koyama; J Michael Conlon; Fumiyuki Yamakura; Shawichi Iwamuro
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-07-24
Journal Detail:
Title:  Biochimie     Volume:  90     ISSN:  1638-6183     ISO Abbreviation:  Biochimie     Publication Date:    2008 Nov-Dec
Date Detail:
Created Date:  2008-11-12     Completed Date:  2009-07-08     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  1264604     Medline TA:  Biochimie     Country:  France    
Other Details:
Languages:  eng     Pagination:  1693-702     Citation Subset:  IM    
Department of Biology, Faculty of Science, Toho University, Funabashi, Chiba, Japan.
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MeSH Terms
Carrier Proteins / metabolism
Cloning, Molecular
DNA / metabolism
Escherichia coli / drug effects*
Histones / genetics,  metabolism*,  pharmacology*
Rana esculenta / immunology*
Recombinant Fusion Proteins / genetics,  metabolism,  pharmacology
Skin / immunology*
Subtilisins / metabolism*
Reg. No./Substance:
0/Carrier Proteins; 0/Histones; 0/Recombinant Fusion Proteins; 0/maltose-binding protein; 9007-49-2/DNA; EC 3.4.21.-/Subtilisins; EC 3.4.21.-/proteinase T

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