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

Biochimie
Hiroaki KawasakiShawichi Iwamuro

Abstract

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 o...Continue Reading

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Citations

Aug 26, 2014·Trends in Cell Biology·Paul B Talbert, Steven Henikoff
Sep 5, 2012·The Journal of Cell Biology·Volker Brinkmann, Arturo Zychlinsky
Jul 18, 2015·Pharmaceuticals·Biljana Mojsoska, Håvard Jenssen
Dec 30, 2015·Biochimica Et Biophysica Acta·Chao-Wen Wang
Sep 23, 2009·Peptides·Hoi See TsaoDonald E Elmore
Jan 11, 2012·Biochimica Et Biophysica Acta·Kathryn E PaviaDonald E Elmore
Apr 17, 2021·Cancer Biology & Therapy·Ileana J Fernández-DomínguezCatalina Trejo-Becerril
Apr 26, 2021·Clinical Biochemistry·Mauro MoianaGabriela de Larrañaga

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