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http://purl.uniprot.org/citations/16256065http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16256065http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16256065http://www.w3.org/2000/01/rdf-schema#comment"Long-chain acyl-CoA synthetases (LACSs) activate fatty acids for further metabolism and are encoded by a multi-gene family in Arabidopsis. AtLACS6 possesses a type 2 (PTS2) peroxisomal targeting sequence, whilst AtLACS7 has both a type 1 and type 2 peroxisomal targeting sequence. AtLACS7 was used as bait in a yeast two-hybrid screen. Multiple clones of the PTS1 receptor PEX5 were isolated. Quantitative beta-galactosidase assay indicated that full-length PEX5 interacts with AtLACS7 with higher affinity than the TPR domains alone. The interaction between PEX5 and AtLACS7 was confirmed by co-immunoprecipitation and shown to be specific for the PTS1, therefore the AtLACS7 PTS1 is accessible to bind PEX5 in the full-length AtLACS7 protein. The expression profile of AtLACS6, AtLACS7, AtPEX5, and AtPEX7 revealed that AtLACS6 and 7 have distinct patterns of expression and we speculate that the possession of two targeting signals may be advantageous for the import of AtLACS7 when receptors may be limiting."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2005.09.003"xsd:string
http://purl.uniprot.org/citations/16256065http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2005.09.003"xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Baker A."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Baker A."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Slocombe S.P."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Slocombe S.P."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"De Bellis L."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"De Bellis L."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Bonsegna S."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/author"Bonsegna S."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/pages"74-81"xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/pages"74-81"xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/title"AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/title"AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5."xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/volume"443"xsd:string
http://purl.uniprot.org/citations/16256065http://purl.uniprot.org/core/volume"443"xsd:string
http://purl.uniprot.org/citations/16256065http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16256065
http://purl.uniprot.org/citations/16256065http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16256065