Erschienen in:
The Plant Journal, 32 (2002) 3, Seite 263-276
Sprache:
Englisch
DOI:
10.1046/j.1365-313x.2002.01420.x
ISSN:
0960-7412;
1365-313X
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>Summary</jats:title><jats:p>The <jats:italic>twisted dwarf</jats:italic>1 (<jats:italic>twd</jats:italic>1) mutant from <jats:italic>Arabidopsis thaliana</jats:italic> was identified in a screen for plant architecture mutants. The <jats:italic>TWD1</jats:italic> gene encodes a 42 kDa FK506‐binding protein (<jats:italic>At</jats:italic>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 <jats:italic>Arabidopsis</jats:italic> that consists of <jats:italic>At</jats:italic>Hsp90 and <jats:italic>At</jats:italic>FKBP42. Recombinant <jats:italic>At</jats:italic>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, <jats:italic>At</jats:italic>FKBP42 lacks the PPIase active FKBP domain. While FKBP52 is found in the cytosol and translocates to the nucleus, <jats:italic>At</jats:italic>FKBP42 was predicted to be membrane‐localized, as shown by electron microscopy.</jats:p>