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Putative identification of an amphipathic α-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation
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Angela Valeva
Published/Copyright:
August 19, 2008
Abstract
Escherichia coli hemolysin is a pore-forming protein belonging to the RTX toxin family. Cysteine scanning mutagenesis was performed to characterize the putative pore-forming domain of the molecule. A single cysteine residue was introduced at 48 positions within the sequence spanning residues 170–400 and labeled with the polarity-sensitive dye badan. Spectrofluorimetric analyses indicated that several amino acids in this domain are inserted into the lipid bilayer during pore formation. An amphipathic α-helix spanning residues 272–298 was identified that may line the aqueous pore. The importance of this sequence was highlighted by the introduction of two prolines at positions 284 and 287. Disruption of the helix structure did not affect binding properties, but totally abolished the hemolytic activity of the molecule.
Keywords: amphipathic α-helix-lined pore; fluorescence spectroscopy; protein-membrane interaction; RTX toxin
Received: 2008-3-5
Accepted: 2008-5-19
Published Online: 2008-08-19
Published in Print: 2008-09-01
©2008 by Walter de Gruyter Berlin New York
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Keywords for this article
amphipathic α-helix-lined pore;
fluorescence spectroscopy;
protein-membrane interaction;
RTX toxin
Articles in the same Issue
- Review
- Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
- Protein Structure and Function
- The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme
- Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGAP interaction
- Docking of tryptophan analogs to trytophanyl-tRNA synthetase: implications for non-canonical amino acid incorporations
- Molecular mechanisms of aromatase inhibition by new A, D-ring modified steroids
- A common binding motif for various bacteria of the bacteria-binding peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin
- Putative identification of an amphipathic α-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation
- Proteolysis
- Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
- Cleaved SLPI, a novel biomarker of chymase activity
- Expression of tissue and plasma kallikreins and kinin B1 and B2 receptors in lung cancer
- Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
- Novel Techniques
- Fast in vitro translation system immobilized on a surface via specific biotinylation of the ribosome
