Reference: Griffin EE and Chan DC (2006) Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion. J Biol Chem 281(24):16599-606

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Abstract


Mitofusins are conserved GTPases essential for the fusion of mitochondria. These mitochondrial outer membrane proteins contain a GTPase domain and two or three regions with hydrophobic heptad repeats, but little is known about how these domains interact to mediate mitochondrial fusion. To address this issue, we have analyzed the yeast mitofusin Fzo1p and find that mutation of any of the three heptad repeat regions (HRN, HR1, and HR2) leads to a null allele. Specific pairs of null alleles show robust complementation, indicating that functional domains need not exist on the same molecule. Biochemical analysis indicates that this complementation is due to Fzo1p oligomerization mediated by multiple domain interactions. Moreover, we find that two non-overlapping protein fragments, one consisting of HRN/GTPase and the other consisting of HR1/HR2, can form a complex that reconstitutes Fzo1p fusion activity. Each of the null alleles disrupts the interaction of these two fragments, suggesting that we have identified a key interaction involving the GTPase domain and heptad repeats essential for fusion.

Reference Type
Journal Article | Research Support, N.I.H., Extramural
Authors
Griffin EE, Chan DC
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Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 1 entry for 1 gene

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InteractorInteractorAssayAnnotationActionModification
FZO1FZO1Affinity Capture-Westernmanually curatedHit-BaitNo Modification
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