Source:http://linkedlifedata.com/resource/pubmed/id/10972879
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2000-11-14
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pubmed:abstractText |
KAT1 and AKT1 belong to the multigenic family of the inwardly rectifying Shaker-like plant K+ channels. They were biochemically characterized after expression in insect cells using recombinant baculoviruses. The channels were solubilized from microsomal fractions prepared from infected cells (among eight different detergents only one, L-alpha-lysophosphatidylcholine, was efficient for solubilization), and purified to homogeneity using immunoaffinity (KAT1) or ion-exchange and size exclusion (AKT1) techniques. The following results were obtained with the purified polypeptides: (i) neither KAT1 nor AKT1 was found to be glycosylated; (ii) both polypeptides were mainly present as homotetrameric structures, supporting the hypothesis of a tetrameric structure for the functional channels; (iii) no heteromeric KAT1/AKT1 assembly was detected when the two polypeptides were co-expressed in insect cells. The use of the two-hybrid system in yeast also failed to detect any interaction between KAT1 and AKT1 polypeptides. Because of these negative results, the hypothesis that plant K+-channel subunits are able to co-assemble without any discrimination, previously put forward based on co-expression in Xenopus oocytes of various K+-channel subunits (including KAT1 and AKT1), has still to be supported by independent approaches. Co-localization of channel subunits within the same plant tissue/cell does not allow us to conclude that the subunits form heteromultimeric channels.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AKT1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/KAT1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-38
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10972879-Animals,
pubmed-meshheading:10972879-Arabidopsis,
pubmed-meshheading:10972879-Arabidopsis Proteins,
pubmed-meshheading:10972879-Baculoviridae,
pubmed-meshheading:10972879-Blotting, Western,
pubmed-meshheading:10972879-Cell Extracts,
pubmed-meshheading:10972879-Cell Line,
pubmed-meshheading:10972879-Chromatography, Affinity,
pubmed-meshheading:10972879-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10972879-Glycosylation,
pubmed-meshheading:10972879-Insects,
pubmed-meshheading:10972879-Plant Proteins,
pubmed-meshheading:10972879-Potassium Channels,
pubmed-meshheading:10972879-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:10972879-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
Biochemical characterization of the Arabidopsis K+ channels KAT1 and AKT1 expressed or co-expressed in insect cells.
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pubmed:affiliation |
Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, UMR 5004, Agro-M/CNRS/INRA/UMII, 34060 Montpellier Cedex 1, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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