BAIT

CPL1

ATCPL1, ATCPL2, C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1, F17L22.130, F17L22_130, FIERY 2, FRY2, AT4G21670
RNA polymerase II C-terminal domain phosphatase-like 1
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

Fast-forward genetics identifies plant CPL phosphatases as regulators of miRNA processing factor HYL1.

Manavella PA, Hagmann J, Ott F, Laubinger S, Franz M, Macek B, Weigel D

MicroRNAs (miRNAs) are processed from primary transcripts that contain partially self-complementary foldbacks. As in animals, the core microprocessor in plants is a Dicer protein, DICER-LIKE1 (DCL1). Processing accuracy and strand selection is greatly enhanced through the RNA binding protein HYPONASTIC LEAVES 1 (HYL1) and the zinc finger protein SERRATE (SE). We have combined a luciferase-based genetic screen with whole-genome sequencing ... [more]

Cell Nov. 09, 2012; 151(4);859-70 [Pubmed: 23141542]

Throughput

  • Low Throughput

Additional Notes

  • BiFC
  • Figure 3

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CPL1 SE
Two-hybrid
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.

Low-BioGRID
1112572

Curated By

  • BioGRID