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Expression data from Arabidopsis wild-type (Col-0) and KO-nudx19 plants, which lacks nudix hydrolase 19, a NADPH hydrolase

ABSTRACT: The NADPH status, which is regulated by AtNUDX19, a NADPH pyrophosphohydrolase, is involved in the regulation of stress and hormonal responses. To clarify how the status is involved in the regulation, we performed a microarray analysis using 3-week-old wild-type and KO-nudx19 leaves grown under normal light conditions.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE64968 | GEO | 2015/01/15

SECONDARY ACCESSION(S): PRJNA272608

REPOSITORIES: GEO

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Expression data from Arabidopsis wild-type (Col-0) and KO-nudx19 plants, which lacks nudix hydrolase 19, a NADPH hydrolase

Project description:The NADPH status, which is regulated by AtNUDX19, a NADPH pyrophosphohydrolase, is involved in the regulation of stress and hormonal responses. To clarify how the status is involved in the regulation, we performed a microarray analysis using 3-week-old wild-type and KO-nudx19 leaves grown under normal light conditions. Wild-type and KO-nudx19 plants were grown on MS medium containing 3% sucrose in a growth chamber kept at 25Â°C during 16 h of light (100 Âµmol/m2/s) and at 22Â°C during 8 h of darkness for 1 week, and then transferred to and further grown on soil for 2 weeks in the same chamber. At 3 weeks, leaves were collected as samples for microarray analysis.

2015-01-15 | E-GEOD-64968 | biostudies-arrayexpress

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Project description:NADPH has been long well-recognized as a key cofactor for antioxidant defense and reductive biosynthesis. Here we report a metabolism-independent function of NADPH in modulating epigenetic status and transcription. We found that reduction of cellular NADPH levels by silencing malic enzyme (ME) or G6PD impairs global histone acetylation and transcription in both adipocytes and tumor cells. These effects can be reversed by supplementation of exogenous NADPH or inhibition of histone deacetylase 3 (HDAC3). Mechanistically, NADPH or inhibition of histone deacetylase 3 (HDAC3). Mechanistically,NADPH directly interacts with HDAC3 and interrupts the association between HDAC3 and its co-activator Ncor2 (SMRT) or Ncor1, thereby impairs HDAC3 activation. Interestingly, it appears that NADPH and Ins(1,4,5,6)P4 bind to the same domains on HDAC3, and NADPH has relatively higher affinity towards HDAC3. Thus, while Ins(1,4,5,6)P4 acts as an ‘intermolecular glue’, NADPH may function as a HDAC3-Ncor assembly inhibitor. Collectively, our findings uncovered a previous unidentified and metabolism-independent role of NADPH in controlling epigenetic change and gene expression by acting as an endogenous inhibitor of HDAC3.

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2012-03-31 | E-GEOD-34810 | biostudies-arrayexpress

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