http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9182
The phytotoxic lipodepsipeptide syringopeptin 25A from Pseudomonas syringae pv syringae forms ion channels in sugar beet vacuoles (Articolo in rivista)
- Type
- Label
- The phytotoxic lipodepsipeptide syringopeptin 25A from Pseudomonas syringae pv syringae forms ion channels in sugar beet vacuoles (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00232-001-0187-x (literal)
- Alternative label
Carpaneto A., Dalla Serra M., Menestrina G., Fogliano V., Gambale F. (2002)
The phytotoxic lipodepsipeptide syringopeptin 25A from Pseudomonas syringae pv syringae forms ion channels in sugar beet vacuoles
in The journal of membrane biology (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Carpaneto A., Dalla Serra M., Menestrina G., Fogliano V., Gambale F. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR, Ist Biofis, I-16149 Genoa, Italy
CNR, ITC, IBF, Ctr Fis Stati Aggregati, I-38050 Povo, Trento, Italy
Univ Naples Federico II, Dipartimento Sci Alimenti, I-80138 Naples, Italy (literal)
- Titolo
- The phytotoxic lipodepsipeptide syringopeptin 25A from Pseudomonas syringae pv syringae forms ion channels in sugar beet vacuoles (literal)
- Abstract
- Syringopeptin 25A (SP(25)A) belongs to a family of cyclic
lipodepsipeptides (LDPs) produced by the gram-negative bacterium
Pseudomonas syringae, a phytopathogenic organism that affects several
plants of agronomic interest. LDPs increase the permeability of plasma
and, possibly, intracellular membranes in plant cells. Consistently, SP
(25)A forms ion channels in planar lipid bilayers and other model
membranes.
Here we used sugar beet tonoplasts as a new biological model system to
study toxin action. When applied to the vacuoles by a fast perfusion
procedure, SP(25)A increases membrane permeability by forming discrete
ion channels even at low applied potentials. The SP(25)A channel displays
anion selectivity (with a Cl-/K+ permeability ratio of 6.7 +/- 1.3) and
has intrinsic rectification properties that derive from a different
channel conductance at negative and positive voltages, presumably owing
to an asymmetric distribution of fixed charges on the pore. Substitution
of chloride with different anions reveals the following selectivity
sequence NO3- approximately Cl-> F- > gluconate-, suggesting that the
permeation pore is filled with water. The properties of the SP(25)A
channels in vacuolar membranes are similar to those observed in planar
lipid membranes prepared with asolectin. This work provides a direct
demonstration of toxin effects on a native plant membrane, extending to a
biological system previous results obtained on artificial planar lipid
membranes. (literal)
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