| http://purl.uniprot.org/citations/16236153 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16236153 | http://www.w3.org/2000/01/rdf-schema#comment | "The endoplasmic reticulum-associated oleate desaturase FAD2 (1-acyl-2-oleoyl-sn-glycero-3-phosphocholine Delta12-desaturase) is the key enzyme responsible for the production of linoleic acid in non-photosynthetic tissues of plants. Little is known, however, concerning the post-transcriptional mechanisms that regulate the activity of this important enzyme. The soybean genome possesses two seed-specific isoforms of FAD2, designated FAD2-1A and FAD2-1B, which differ at only 24 amino acid residues. Expression studies in yeast revealed that the FAD2-1A isoform is more unstable than FAD2-1B, particularly when cultures were maintained at elevated growth temperatures. Analysis of chimeric FAD2-1 constructs led to the identification of two domains that appear to be important in mediating the temperature-dependent instability of the FAD2-1A isoform. The enhanced degradation of FAD2-1A at high growth temperatures was partially abrogated by treating the cultures with the 26S proteasome-specific inhibitor MG132, and by expressing the FAD2-1A cDNA in yeast strains devoid of certain ubiquitin-conjugating activities, suggesting a role for ubiquitination and the 26S proteasome in protein turnover. In addition, phosphorylation state-specific antipeptide antibodies demonstrated that the Serine-185 of FAD2-1 sequences is phosphorylated during soybean seed development. Expression studies of phosphopeptide mimic mutations in yeast suggest that phosphorylation may downregulate enzyme activity. Collectively, the results show that post-translational regulatory mechanisms are likely to play an important role in modulating FAD2-1 enzyme activities."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1365-313x.2005.02535.x"xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/author | "Dewey R.E."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/author | "Huber S.C."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/author | "Tang G.Q."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/author | "Novitzky W.P."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/author | "Carol Griffin H."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/name | "Plant J"xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/pages | "433-446"xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/title | "Oleate desaturase enzymes of soybean: evidence of regulation through differential stability and phosphorylation."xsd:string |
| http://purl.uniprot.org/citations/16236153 | http://purl.uniprot.org/core/volume | "44"xsd:string |
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