BAIT

TOC159

ATTOC159, PLASTID PROTEIN IMPORT 2, PPI2, T10P11.19, TOC160, TOC86, TRANSLOCON AT THE OUTER ENVELOPE MEMBRANE OF CHLOROPLASTS 160, TRANSLOCON AT THE OUTER ENVELOPE MEMBRANE OF CHLOROPLASTS 86, translocon at the outer envelope membrane of chloroplasts 159, AT4G02510
translocase of chloroplast 159
GO Process (1)
GO Function (3)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

NPQ4

CP22, NONPHOTOCHEMICAL QUENCHING 4, PHOTOSYSTEM II SUBUNIT S, PSBS, PSII-S, T18F15.3, T18F15_3, AT1G44575
photosystem II subunit S
Arabidopsis thaliana (Columbia)

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.

Publication

A Split-Ubiquitin Yeast Two-Hybrid Screen to Examine the Substrate Specificity of atToc159 and atToc132, Two Arabidopsis Chloroplast Preprotein Import Receptors.

Dutta S, Teresinski HJ, Smith MD

Post-translational import of nucleus-encoded chloroplast pre-proteins is critical for chloroplast biogenesis, and the Toc159 family of proteins serve as receptors for the process. Toc159 shares with other members of the family (e.g. Toc132), homologous GTPase (G-) and Membrane (M-) domains, but a highly dissimilar N-terminal acidic (A-) domain. Although there is good evidence that atToc159 and atToc132 from Arabidopsis mediate ... [more]

PLoS ONE Apr. 17, 2014; 9(4);e95026 [Pubmed: 24736607]

Throughput

  • High Throughput

Additional Notes

  • Split-ubiquitin assay
  • atToc159G bait protein

Curated By

  • BioGRID