Construction and characterisation of yeast mutants with modified inhibitor
binding sites in cytochrome b.
A three year postdoctoral position will be available in our group to work
on cytochrome b mutations in yeast. Enquiry and application should be
addressed to Dr Brigitte Meunier <b.meunier at ucl.ac.uk>. The Wolfson
Institute for Biomedical Research, University College London.
The mitochondrial bc1 complex is a membrane-bound enzyme, composed of up to
eleven subunits, that catalyses the transfer of electrons from ubiquinol
to cytochrome c and couples this electron transfer process to the
translocation of protons across the inner mitochondrial membrane. The
mitochondrially-encoded cytochrome b in concert with cytochrome c1 and the
Rieske protein, forms the catalytic core of the enzyme. Inhibitors of the
bc1 complex which are widely used as fungicides in agriculture, interact
with the quinol binding site of cytochrome b. Inhibitor resistance caused
by cytochrome b mutations has been observed in plant pathogen fungi.
As saccharomyces cerevisiae is amenable to mitochondrial transformation, it
is possible to introduce designed mutations in cytochrome b. In this
project, we will modify the inhibitor binding pocket of the yeast enzyme to
mimic the structure of plant pathogen sites. The yeast mutants with new
forms of bc1 complex will then be used as (easy to manipulate) models to
study inhibitor resistance.
for Biomedical Research
University College London