Reference: Goping IS, et al. (1995) Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of delta mas20 in yeast. FEBS Lett 373(1):45-50

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Abstract


The human homolog of the S. cerevisiaelN. crassa mitochondrial protein import receptor, Mas20p/MOM19, has been identified and characterized. Sequence similarities between these three proteins is most pronounced within the NH2-terminal third of the molecules. However, the mammalian protein exhibits only weak homology to the tetratricopeptide repeat B domain that is found in Mas20p/MOM19. huMas20p is targeted and inserted into the outer membrane of isolated rat heart mitochondria, in the Nin-Ccyto orientation. Antibodies directed against the soluble portion of huMas20p inhibited in vitro mitochondrial import of a diverse set of precursor proteins (including inner membrane uncoupling protein), but failed to block import of a fusion protein bearing the signal-anchor sequence of Mas20p itself. Finally, expression of huMAS20 complemented the respiratory defect of delta mas20 yeast cells. Together, these results demonstrate that huMAS20p is a component of the mammalian import apparatus.

Reference Type
Comparative Study | Journal Article | Research Support, Non-U.S. Gov't
Authors
Goping IS, Millar DG, Shore GC
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