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Comparison of the N-terminal tail of the human and yeast Fis1 protein. The yeast Fis1 N-terminal sits in the hydrophobic groove of the protein. The hydrophobic interaction between the N-terminal tail and the groove is complemented by electrostatic interactions at the its perimeter. Truncation of this N-terminal tail abolishes Mdv1 recruitment to the mitochondria membrane, thus inhibiting mitochondria fission. This is illustrated by the diffuse profile of the GFP-Mdv1 confocal in yeast transfected with N-terminal truncated Fis1.
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