The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain.

LETM1 is a mitochondrial inner membrane protein that is required for maintaining the mitochondrial morphology and cristae structures, and regulates mitochondrial ion homeostasis. Here we report a role of LETM1 in the organization of cristae structures. We identified four amino acid residues of human LETM1 that are crucial for complementation of the growth deficiency caused by gene deletion of a yeast LETM1 orthologue.

In vitro synthesis of the human calcium transporter Letm1 within cell-sized liposomes and investigation of its lipid dependency.

The human mitochondrion-derived calcium transporter Letm1 was synthesized by reconstituted in vitro transcription-translation (IVTT) in cell-sized liposomes and the dependency of Letm1 on phospholipid composition was investigated. Components for IVTT were encapsulated into cell-sized vesicles together with the DNA encoding Letm1, thereby preparing proteoliposomes. The synthesis of Letm1 and pH-dependent calcium transport activity were confirmed by flow cytometry.

The role of autophagy in genome stability through suppression of abnormal mitosis under starvation.

The coordination of subcellular processes during adaptation to environmental change is a key feature of biological systems. Starvation of essential nutrients slows cell cycling and ultimately causes G1 arrest, and nitrogen starvation delays G2/M progression. Here, we show that budding yeast cells can be efficiently returned to the G1 phase under starvation conditions in an autophagy-dependent manner.

Cell size regulation during telomere-directed senescence in Saccharomyces cerevisiae.

DNA replication without telomerase leads to telomere shortening and induces replicative senescence. We found that in a telomerase-deficient budding yeast mutant, the volume of each telomere-shortened cell increased as its growth capacity decreased, and that this process was associated with changes in vacuolar morphology. Senescence-induced cell expansion required Mec1, a DNA damage-responsive kinase, but not vacuolar SNARE Vam3.