tailieunhanh - Báo cáo khóa học: Processing of the 24 kDa subunit mitochondrial import signal is not required for assembly of functional complex I in Yarrowia lipolytica

A small deletion in the second intron of humanNDUFV2 (IVS2+5_+8delGTAA) has been shown to cause hyper-trophic cardiomyopathy and encephalomyopathy [Be´nit, P., Beugnot, R., Chretien, D., Giurgea, I., de Lonlay-Debeney, P., Issartel, ., Kerscher, S., Rustin, P., Ro¨tig, A. & Munnich, A. (2003)Human , 582–586]. Skipping of exon 2 results in a partial deletion of the mitochondrial targeting sequence of the precursor for the 24 kDa subunit of respiratory chain complex I. | Eur. J. Biochem. 271 3588-3595 2004 FEBS 2004 doi Processing of the 24 kDa subunit mitochondrial import signal is not required for assembly of functional complex I in Yarrowia lipolytica Stefan Kerscher1 Paule Benit2. Albina Abdrakhmanova1 Klaus Zwicker1 Isam Rais3. Michael Karas3 B F BF B 4 w BF B BB BBB B BF B B BB w B BB B B B B B B B B B B B B BB B B B B B B BB B B Bb w BB B w B BB B BB V V B VBB w B B BB BB B B B B B BB B BB B B B B B B BB B B w BB B BB BB Pierre Rustin2 and Ulrich Brandt1 1 Universitat Frankfurt Fachbereich Medizin Institut fur Biochemie I Frankfurt am Main Germany 2INSERM U393 Hopital Necker-Enfants Malades Paris France 3 Universităt Frankfurt Institut fur Pharmazeutische Chemie Frankfurt am Main Germany A small deletion in the second intron of human NDUFV2 IVS2 5_ 8delGTAA has been shown to cause hypertrophic cardiomyopathy and encephalomyopathy Benit P. Beugnot R. Chretien D. Giurgea I. de Lonlay-Debeney P. Issartel . Kerscher S. Rustin P. Rotig A. Munnich A. 2003 Human Mutat. 21 582-586 . Skipping of exon 2 results in a partial deletion of the mitochondrial targeting sequence of the precursor for the 24 kDa subunit of respiratory chain complex I. Immunoreactivity of the 24 kDa subunit and complex I activity both present at 30-50 of normal levels in patient mitochondria raised the question of how the mutant 24 kDa subunit precursor can be imported and assembled into functional complex I. In the present study we have remodelled the human NDUFV2 mutation by deleting codons 17-32 from the orthologous NUHM gene of the obligate aerobic yeast Yarrowia lipo-lytica. The resulting mutant enzyme was indistinguishable from parental complex I with regard to activity inhibitor sensitivity and EPR signature. Size isoelectric point and presumably also N-terminal acetylation were altered indicating that the residual targeting sequence was retained on the mature 24 kDa protein. Complete removal of the NUHM presequence .

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