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An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting protein) in an interaction that is disrupted by FK506
Author(s) -
Faure JeanDenis,
Gingerich Derek,
Howell Stephen H.
Publication year - 1998
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1998.00248.x
Subject(s) - fkbp , arabidopsis , biology , fusion protein , arabidopsis thaliana , peptidylprolyl isomerase , binding protein , two hybrid screening , complementary dna , cyclophilin , biochemistry , plasma protein binding , protein–protein interaction , microbiology and biotechnology , yeast , gene , mutant , recombinant dna , isomerase
Summary AtFKBP12 is an Arabidopsis cDNA that encodes a protein similar to the mammalian immunophilin, FKBP12. AtFKBP12 was used as ‘bait’ in a yeast 2‐hybrid system to screen for cDNAs in Arabidopsis encoding proteins that bind to FKBP12. Two partial cDNAs were recovered encoding the C‐terminus of a protein we have calledArabidopsis thalianaFKBP12 interacting protein 37 (AtFIP37). AtFIP37 is similar to a mammalian protein, FAP48, that also binds to FKBP12. The interaction between AtFKBP12 and AtFIP37 in the 2‐hybrid system, as assessed by histidine auxotrophy and β‐galactosidase activity, was disrupted by FK506, but not by cyclosporin A, a drug that binds to cyclophilin A. AtFIP37 was also shown to bindin vitroto AtFKBP12 in GST‐fusion protein binding assays. The binding was abolished by prior incubation of AtFKBP12 with FK506. These findings indicate that an Arabidopsis FKBP12 ortholog encodes a protein that binds FK506 and that the interaction between AtFKBP12 and AtFIP37 may involve the FK506 binding site of AtFKBP12. The interaction provides interesting new opportunities for controlling protein:protein interactionsin vivoin plants.