MWP19.3, glucose-6-phosphate dehydrogenase 1, AT5G35790
glucose-6-phosphate dehydrogenase 1
GO Process (2)
GO Function (2)
GO Component (2)

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)


F9H3.15, F9H3_15, T5L23.1, AT4G03520
thioredoxin M2
GO Process (2)
GO Function (1)
GO Component (5)
Arabidopsis thaliana (Columbia)


A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.


Alternative targeting of Arabidopsis plastidic glucose-6-phosphate dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in the cytosol.

Meyer T, Hoelscher C, Schwoeppe C, von Schaewen A

Arabidopsis peroxisomes contain an incomplete oxidative pentose-phosphate pathway (OPPP), consisting of 6-phosphogluconolactonase and 6-phosphogluconate dehydrogenase isoforms with peroxisomal targeting signals (PTS). To start the pathway, glucose-6-phosphate dehydrogenase (G6PD) is required; however, G6PD isoforms with obvious C-terminal PTS1 or N-terminal PTS2 motifs are lacking. We used fluorescent reporter fusions to explore possibly hidden peroxisomal targeting information. Among the six Arabidopsis G6PD ... [more]

Unknown Feb. 11, 2011; 0(0); [Pubmed: 21309870]


  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.


Curated By

  • BioGRID