Specific photoaffinity labelling of a ferripyoverdin outer membrane receptor ofPseudomonas aeruginosa

Autor: Christophe Hennard, Mohamed A. Abdallah, Anthony W. Smith, Caroline Linget-Morice, Peter A. Lambert, Pavel Kyslík, Isabelle J. Schalk, Aydin Z. Ocaktan
Přispěvatelé: Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Laboratory of Enzyme Technology, Czech Academy of Sciences [Prague] (ASCR), School of Life and Heath Sciences, Aston University [Birmingham], Schalk, Isabelle, Czech Academy of Sciences [Prague] (CAS)
Rok vydání: 1996
Předmět:
Siderophore
Siderophores
Biochemistry
Structural Biology
Receptor
Polyacrylamide gel electrophoresis
MESH: Iron
0303 health sciences
Oligopeptide
MESH: Kinetics
biology
Chemistry
Affinity Labels
Pseudomonas aeruginosa
MESH: Oligopeptides
MESH: Pseudomonas aeruginosa
Electrophoresis
Polyacrylamide Gel
Pyoverdin
Bacterial outer membrane
Oligopeptides
Bacterial Outer Membrane Proteins
MESH: Pigments
Biological
Azides
Ultraviolet Rays
Iron
Affinity label
Biophysics
Azidopyoverdin
03 medical and health sciences
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology
Genetics
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH: Siderophores
Iron transport
Molecular Biology
Ion transporter
030304 developmental biology
MESH: Affinity Labels
Ion Transport
Molecular mass
030306 microbiology
MESH: Bacterial Outer Membrane Proteins
Pigments
Biological
Cell Biology
MESH: Azides
Photoaffinity labelling
MESH: Ion Transport
Kinetics
Outer membrane receptor
biology.protein
MESH: Ultraviolet Rays
MESH: Electrophoresis
Polyacrylamide Gel
Zdroj: FEBS Letters
FEBS Letters, Wiley, 1996, 396 (2-3), pp.243-7
ISSN: 0014-5793
1873-3468
DOI: 10.1016/0014-5793(96)01071-x
Popis: In order to identify and characterize the receptors involved in pyoverdin-mediated iron transport in Pseudomonas aeruginosa ATCC 15692, a photoactivatable siderophore has been synthesized. In the dark, this probe is stable and is able to promote iron transport at the same rate as the native pyoverdin. Under irradiation at 312 nm, the molecule is photodecomposed and a clear inhibition of the iron transport is observed. With the radioactive form of this photoactivatable probe, we were able to visualize on a SDS-PAGE gel a labelled protein of approximately 90 kDa molecular mass, which is very likely the FpvA receptor or a yet unknown pyoverdin receptor.
Databáze: OpenAIRE
Externí odkaz: