Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Interaction of Escherichia coli hemolysin with biological membranes - A study using cysteine scanning mutagenesis
Autore:
Schindel, C; Zitzer, A; Schulte, B; Gerhards, A; Stanley, P; Hughes, C; Koronakis, V; Bhakdi, S; Palmer, M;
Indirizzi:
Univ Mainz, Inst Med Mikrobiol & Hyg, D-55101 Mainz, Germany Univ Mainz Mainz Germany D-55101 Mikrobiol & Hyg, D-55101 Mainz, Germany Univ Cambridge, Dept Pathol, Cambridge CB2 1TN, England Univ Cambridge Cambridge England CB2 1TN hol, Cambridge CB2 1TN, England
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 268, anno: 2001,
pagine: 800 - 808
SICI:
0014-2956(200102)268:3<800:IOECHW>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ERYTHROCYTE-MEMBRANES; FATTY ACYLATION; ALPHA-HEMOLYSIN; BINDING; PORE; PROTEIN; CALCIUM; TOXIN; HLYA; DOMAIN;
Keywords:
badan; calcium; conformation; Escherichia coli hemolysin, membrane;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Schindel, C Univ Mainz, Inst Med Mikrobiol & Hyg, Hochhaus Augustuspl, D-55101 Mainz, Germany Univ Mainz Hochhaus Augustuspl Mainz Germany D-55101 Germany
Citazione:
C. Schindel et al., "Interaction of Escherichia coli hemolysin with biological membranes - A study using cysteine scanning mutagenesis", EUR J BIOCH, 268(3), 2001, pp. 800-808

Abstract

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2+ to the C-terminus, of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blueshift in the emission of six residues within the N-terminal hydrophobic domain, indicating insertion of this domain into the lipid bilayer. The emission shifts occurred both in the presence and absence of Ca2+, suggesting that Ca2+ is not required for the toxin to enter membranes. However, binding of Ca2+ to HlyA in solution effected conformational changes in both the C-terminal and N-terminal domain that paralleled activation. Our data indicatethat binding of Ca2+ to the toxin in solution effects a conformational change that is relayed to the N-terminal domain, rendering it capable of adopting the structure of a functional pore upon membrane binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 09:03:22