A salaried research position is available at the Ohio State University in
the Department of Plant Cellular and Molecular Biology in Dr Patrice Hamel's
hamel_lab.htm). The position is for one year and starts on September 1 (date
is flexible). We wish to recruit a student with some laboratory experience
(BS or MS or eq. for instance) to study mitochondrial complex I assembly in
the green alga Chlamydomonas (see below for a scientific summary of the
project). Future hire will be exposed to molecular genetic and biochemistry
techniques and will work in close interaction with a graduate student.
Applicants can email Dr Hamel (hamel.16 from osu.edu).
Many human pathologies such as myopathies and neurodegenerative disorders
like Parkinson's disease are associated with dysfunction of the
mitochondria. Among the most prevalent forms of mitochondrial dysfunction
(with an estimated incidence of 1 in 10,000 live births) are human
deficiencies in complex I, a multimeric enzyme of the respiratory chain.
With over 40 nucleus- and mitochondria-encoded subunits, one FMN molecule
and 8 Fe-S clusters, mitochondrial complex I or NADH-ubiquinone
oxido-reductase is the largest respiratory complex in the mitochondrial
inner membrane. The fact that, in 60% of cases, patients with complex I
defects carry no mutations in the structural genes suggests that mutations
in yet-to-be discovered assembly factors of complex I are important causes
of disease. We propose to study complex I assembly in the single-celled
green alga Chlamydomonas reinhardtii. Chlamydomonas mutants lacking complex
I are amenable to studies because they are viable and display a slow growth
in the dark. Our goals are: 1) clone the AMC1 and AMC2 genes from existing
amc1 and amc2 nuclear mutants (amc for assembly of mitochondrial complex I)
that display a complex I defect and carry out the functional analysis of
their gene products and 2) generate a collection of insertional mutants only
deficient for complex I assembly with the objective to discover novel
nuclear-encoded complex I assembly factors.