BAIT

CR88

AtHsp90.5, EMB1956, EMBRYO DEFECTIVE 1956, F3C11.14, F3C11_14, HEAT SHOCK PROTEIN 88.1, HEAT SHOCK PROTEIN 90.5, HSP90.5, Hsp88.1, AT2G04030
chloroplast heat shock protein 90
Arabidopsis thaliana (Columbia)
PREY

PTAC4

T8F5.2, T8F5_2, VESICLE-INDUCING PROTEIN IN PLASTIDS 1, VIPP1, plastid transcriptionally active 4, AT1G65260
plastid transcriptionally active 4
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

Chloroplast-targeted Hsp90 plays essential roles in plastid development and embryogenesis in Arabidopsis possibly linking with VIPP1.

Feng J, Fan P, Jiang P, Lv S, Chen X, Li Y

The Arabidopsis genome contains seven members of Hsp90. Mutations in plastid AtHsp90.5 were reported to cause defects in chloroplast development and embryogenesis. However, the exact function of plastid AtHsp90.5 has not yet been defined. In this study, albino seedlings were found among AtHsp90.5 transformed Arabidopsis, which were revealed to be AtHsp90.5 co-suppressed plants. The accumulation of photosynthetic super-complexes in the ... [more]

Physiol Plant Jul. 22, 2013; 0(0); [Pubmed: 23875936]

Throughput

  • Low Throughput

Curated By

  • BioGRID