Abstract
In yeast, the GTPase s-mgm1 is responsible for the fusion of inner mitochondrial membranes, a process essential for maintenance of normal mitochondrial morphology and function. Direct, real-time visualization of the effects of s-mgm1 upon mitochondrial mimic membranes is particularly relevant to elucidating the mechanism by which it acts. Here, we utilize both confocal microscopy and AFM to demonstrate that s-mgm1 spontaneously induces GTP-independent pinching and tubulation of lipids in the gel phase. Subsequent addition of GTP causes further remodelling of the membrane. Similar experiments using ATR-FTIR suggest that the membrane induces increased order in protein conformation. Our data is consistent with a model by which s-mgm1 promotes fusion of opposing membranes by pinching and tubulation.
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