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Most chloroplast proteins are synthesized as preproteins in the
cytosol and their import is mediated by molecular complexes located
at the outer and inner membrane of the chloroplast. These complexes
are called TOC (Translocon at the Outer envelope of the
Chloroplast) and TIC (Translocon at the Inner envelope of the
Chloroplast). In Arabidopsis thaliana, the TOC complex consists of
three components: two homologous receptor GTPases, atToc159 and
atToc33 and a protein-import channel, atToc75. During import, the
two GTPases undergo complex interactions although precise
mechanisms remain unknown. In vitro studies revealed that Toc159
and Toc33 interact with each other via dimerisation. According to
the crystal structure of psToc34 homodimer and based on the
G-domain homology of TOC GTPases it is likely that the process of
dimerisation is a key step for chloroplast preprotein import. This
work intends to identify a mutant of Toc159 which dimerisation with
toc33 is increased. Thus, Toc159 D919V was identified and revealed
to bind strongly to Toc33, hydrolyse GTP and complement the TOC159
null mutant. This mutant is promising for further crystallisation
and TAP-tag purification studies.
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