GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
|Status||Page||User||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|RAT:PLPL9||Michelel, MichSt14A 16||2014-04-03 23:10:19 CDT||GO:0090435 protein localization to nuclear envelope (P)||PMID:9490642||ECO:0000314 direct assay evidence used in manual assertion|
Figure 4 shows that when PLA2-I was stained, fluorescence was only detected in the nucleus using confocal and phase contrast microscopy. There was no fluorescence and therefore no protein present anywhere else in the cell.
|9STRA:V5RGX6||Michelel, MichSt14A 16||2014-04-03 20:47:09 CDT||GO:0045723 positive regulation of fatty acid biosynthetic process (P)||PMID:24162136||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 2C shows that when cloned into S. cerevisiae, the protein AUREO1 from N. gaditana significantly increased the amount of lipids in the cell compared to the empty vector.
Figure 2D shows that the S. cerevisiae mutant expressing the gene has increased expression of ACC1 and DGAT and decreased expression of LACS, genes that increase and decrease fatty acid production respectively, indicating that the increased lipid contents were due to this regulation. The empty vector did not affect expression of the fatty acid synthesis genes.
|SYNE7:CMPA||Michelel, MichSt14A 16||2014-04-03 14:34:23 CDT||GO:0015106 bicarbonate transmembrane transporter activity (F)||PMID:10557362||ECO:0000314 direct assay evidence used in manual assertion|
Figure 3 shows that when a mutant placing the cmpABCD ABC transporter complex after a nitrogen-inducible promoter, the mutant took up high amounts of bicarbonate when grown in high bicarbonate media. Comparatively, the WT grown under these same conditions had a negligible uptake of bicarbonate. When grown in media containing ammonium and high amounts of bicarbonate, the mutant has low bicarbonate uptake because the transporter was not induced by nitrogen, so nothing in the cell is taking up bicarbonate.
|PHATR:L8B080||Michelel, MichSt14A 16||2014-04-03 13:28:23 CDT||GO:0005886 plasma membrane (C)||PMID:23297242||ECO:0000314 direct assay evidence used in manual assertion|
Figure 2 B, C and D show that upon fusing the ptSLC4-2 transporter to GFP, it is shown to be localized to the plasmalemma (the same thing as the plasma membrane). Figure 2C shows that ptSLC4-2 is not localized to the nucleus or the chloroplast, and Figure 2D shows that it is localized instead to the plasmalemma.
|PHATC:B7G7S4||Michelel, MichSt14A 16||2014-04-03 11:38:47 CDT||GO:0003989 acetyl-CoA carboxylase activity (F)||PMID:23621611||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 4 shows that when E. coli is transformed with the P. tricornutum ACCase subunit catalyzing the first committed step of the fatty acid biosynthetic pathway, the neutral lipid content significantly increases. When E. coli was transformed with the empty vector there was no neutral lipid content change compared to untransformed E. coli. Table 1 quantifies the ACCase enzyme activity, showing that the mutant E. coli containing P. tricornutum ACCase has significantly higher ACCase activity compared to the empty vector or the untransformed E. coli.
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