Experiment: | 608 |
Title: | Microarray analysis wild type versus mutant |
Date: | 2012-06-20 |
Description: | Phospholipid biosynthesis is essential for the construction of most eukaryotic cell membranes, but how this process isregulated in plants remains poorly understood. Here, we show that in Arabidopsis thaliana, two Mg2+-dependentphosphatidic acid phosphohydrolases called PAH1 and PAH2 act redundantly to repress phospholipid biosynthesis atthe endoplasmic reticulum (ER). Leaves from pah1 pah2 double mutants contain ;1.8-fold more phospholipid than the wildtype and exhibit gross changes in ER morphology, which are consistent with massive membrane overexpansion. The netrate of incorporation of [methyl-14C]choline into phosphatidylcholine (PC) is ;1.8-fold greater in the double mutant, and thetranscript abundance of several key genes that encode enzymes involved in phospholipid synthesis is increased. Inparticular, we show that PHOSPHORYLETHANOLAMINE N-METHYLTRANSFERASE1 (PEAMT1) is upregulated at the level oftranscription in pah1 pah2 leaves. PEAMT catalyzes the first committed step of choline synthesis in Arabidopsis and definesa variant pathway for PC synthesis not found in yeasts or mammals. Our data suggest that PAH1/2 play a regulatory role inphospholipid synthesis that is analogous to that described in Saccharomyces cerevisiae. However, the target enzymesdiffer, and key components of the signal transduction pathway do not appear to be conserved. |
ftp Link: | ftp Link |
Slide ID | Slide Name | Genetic Background | Tissue | Stock Code | Cel File |
---|---|---|---|---|---|
Craddock_608-1_WT_Rep1_ATH1 | 7780586 | Craddock_608-1_WT_Rep1_ATH1.CEL | |||
Craddock_608-2_WT_Rep2_ATH1 | 7780587 | Craddock_608-2_WT_Rep2_ATH1.CEL | |||
Craddock_608-3_WT_Rep3_ATH1 | 7780588 | Craddock_608-3_WT_Rep3_ATH1.CEL | |||
Craddock_608-4_pah_Rep1_ATH1 | 7780589 | Craddock_608-4_pah_Rep1_ATH1.CEL | |||
Craddock_608-5_pah_Rep2_ATH1 | 7780590 | Craddock_608-5_pah_Rep2_ATH1.CEL | |||
Craddock_608-6_pah_Rep3_ATH1 | 7780591 | Craddock_608-6_pah_Rep3_ATH1.CEL |