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http://purl.uniprot.org/citations/11891260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11891260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11891260http://www.w3.org/2000/01/rdf-schema#comment"Four types of phospholipase D (PLD), PLD alpha, beta, gamma, and delta, have been characterized in Arabidopsis, and they display different requirements for Ca(2+), phosphatidylinositol 4,5-bisphosphate (PIP(2)), substrate vesicle composition, and/or free fatty acids. However, all previously cloned plant PLDs contain a Ca(2+)-dependent phospholipid-binding C2 domain and require Ca(2+) for activity. This study documents a new type of PLD, PLD zeta 1, which is distinctively different from previously characterized PLDs. It contains at the N terminus a Phox homology domain and a pleckstrin homology domain, but not the C2 domain. A full-length cDNA for Arabidopsis PLD zeta 1 has been identified and used to express catalytically active PLD in Escherichia coli. PLD zeta 1 does not require Ca(2+) or any other divalent cation for activity. In addition, it selectively hydrolyzes phosphatidylcholine, whereas the other Arabidopsis PLDs use several phospholipids as substrates. PLD zeta 1 requires PIP(2) for activity, but unlike the PIP(2)-requiring PLD beta or gamma, phosphatidylethanolamine is not needed in substrate vesicles. These differences are described, together with a genomic analysis of 12 putative Arabidopsis PLD genes that are grouped into alpha, beta, delta, gamma, and zeta based on their gene architectures, sequence similarities, domain structures, and biochemical properties."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/author"Qin C."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/author"Qin C."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/pages"1057-1068"xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/pages"1057-1068"xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/title"The Arabidopsis phospholipase D family. Characterization of a calcium-independent and phosphatidylcholine-selective PLD zeta 1 with distinct regulatory domains."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/title"The Arabidopsis phospholipase D family. Characterization of a calcium-independent and phosphatidylcholine-selective PLD zeta 1 with distinct regulatory domains."xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/volume"128"xsd:string
http://purl.uniprot.org/citations/11891260http://purl.uniprot.org/core/volume"128"xsd:string
http://purl.uniprot.org/citations/11891260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11891260
http://purl.uniprot.org/citations/11891260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11891260
http://purl.uniprot.org/citations/11891260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11891260
http://purl.uniprot.org/citations/11891260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11891260
http://purl.uniprot.org/uniprot/Q9T051http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11891260
http://purl.uniprot.org/uniprot/O23078http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11891260
http://purl.uniprot.org/uniprot/Q9T053http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11891260
http://purl.uniprot.org/uniprot/Q9C5Y0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11891260