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SUMMARY:IND1\, a Fe-S protein involved in respiratory complex I biogenesis
 . From Arabidopsis gametogenesis defects to patients with mitochondrial my
 opathies - Mateusz Wydro\, Plant Biochemistry
DTSTART:20120309T130000Z
DTEND:20120309T133000Z
UID:TALK35547@talks.cam.ac.uk
CONTACT:24938
DESCRIPTION:Mitochondria of most eukaryotic species contain a large\, mult
 i-subunit protein complex (NADH:ubiquinone oxidoreductase or Complex I). I
 t plays a central role in oxidative phosphorylation by coupling electron t
 ransfer from NADH to quinone with proton translocation. Biosynthesis of co
 mplex I requires synchronized expression of two genomes: (i) the nuclear g
 enome\, encoding most of the 45 subunits\; (ii) the mitochondrial genome w
 hich encodes 7 – 9 mostly hydrophobic subunits. Although recent years ha
 ve brought significant progress in elucidating the structure of complex I\
 , little is known about the assembly of this complicated complex. IND1\, a
  P-loop NTPase\, Fe-S containing protein\, was originally identified in Ar
 abidopsis thaliana\, however its evolutionary conservation in organisms co
 ntaining complex I suggests a fundamental role in complex I biogenesis. In
  agreement with its phylogenetic distribution\, IND1 has been shown to be 
 required for the effective assembly of complex I\, in yeast Yarrowia lipol
 ytica\, in human cell lines and Arabidopsis. Recently\, mutations in the h
 uman homologue NUBPL were shown to cause a complex I deficiency in a patie
 nt with a mitochondrial myopathy (muscle disease). However\, the mode of I
 ND1 function in complex I biogenesis has not yet been fully elucidated. As
  IND1 is capable of binding a transferable Fe-S\, we first hypothesised th
 at it could play a role in delivering Fe-S to one of eight cluster binding
  sites in the hydrophilic arm of complex I. This hypothesis was tested in 
 vitro. During characterisation of IND1 A. thaliana homologue (INDH)\, we h
 ave observed unusual genetic and phenotypic features of the heterozygous k
 nock-out mutant\, strikingly similar to those observed in mutants in organ
 ellar aminoacyl-tRNA synthetases. This finding led us to revise out hypoth
 esis of the function of IND1 and drew our focus to its role in mt-tRNA met
 abolism. I will present the recently obtained data and propose a new funct
 ion of IND1 in complex I biogenesis.
LOCATION:Department of Plant Sciences\, Large Lecture Theatre
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