BAIT

TED4

ARABIDOPSIS THALIANA HEME OXYGENASE 1, ATHO1, F18A8.4, F18A8_4, GENOMES UNCOUPLED 2, GUN2, HEME OXYGENASE, HEME OXYGENASE 1, HEME OXYGENASE 6, HO1, HY1, HY6, PLASTID HEME OXYGENASE, REVERSAL OF THE DET PHENOTYPE 4, AT2G26670
heme oxygenase 1
Arabidopsis thaliana (Columbia)
PREY

AT5G20140

F5O24.30, F5O24_30
SOUL heme-binding protein
GO Process (0)
GO Function (0)
GO Component (5)
Arabidopsis thaliana (Columbia)

Two-hybrid

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.

Publication

Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis.

Lee HJ, Mochizuki N, Masuda T, Buckhout TJ

The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members. The Arabidopsis cytosolic AtHBP1 (At1g17100) and AtHBP2 (At2g37970) have been shown to bind porphyrins and metalloporphyrins including haem. In contrast to the cytosolic localization of these haem-binding proteins, AtHBP5 (At5g20140) encodes a protein with an N-terminal transit peptide that probably directs targeting to the chloroplast. In ... [more]

J. Exp. Bot. Sep. 01, 2012; 63(16);5967-78 [Pubmed: 22991161]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TED4 AT5G20140
PCA
PCA

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.

Low-BioGRID
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Curated By

  • BioGRID