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Characterization of Arabidopsis thaliana At FKBP42 that is membrane‐bound and interacts with Hsp90
Author(s) -
Kamphausen Thilo,
Fanghänel Jörg,
Neumann Dieter,
Schulz Burkhard,
Rahfeld JensU.
Publication year - 2002
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.2002.01420.x
Subject(s) - fkbp , arabidopsis thaliana , arabidopsis , cytosol , mutant , biology , microbiology and biotechnology , biochemistry , hsp90 , chemistry , gene , heat shock protein , enzyme
Summary The twisted dwarf 1 ( twd 1) mutant from Arabidopsis thaliana was identified in a screen for plant architecture mutants. The TWD1 gene encodes a 42 kDa FK506‐binding protein ( At FKBP42) that possesses similarity to multidomain PPIases such as mammalian FKBP51 and FKBP52, which are known to be components of mammalian steroid hormone receptor complexes. We report here for the first time the stoichiometry and dissociation constant of a protein complex from Arabidopsis that consists of At Hsp90 and At FKBP42. Recombinant At FKBP42 prevents aggregation of citrate synthase in almost equimolar concentrations, and can be cross‐linked to calmodulin. In comparison to one active and one inactive FKBP domain in FKBP52, At FKBP42 lacks the PPIase active FKBP domain. While FKBP52 is found in the cytosol and translocates to the nucleus, At FKBP42 was predicted to be membrane‐localized, as shown by electron microscopy.