Proceedings of the National Academy of Sciences · 2009 · 87 citations · 20 references
Life SciencesBiochemistryMicrobiologyCytoskeletonMembrane BiochemistryMitochondrial BiologyMitochondrial BiochemistryMitochondrial MembranesMitochondrial StructureMitochondrial UltrastructureOrganelle BiochemistryOrganelle BiologyBacterial Cell Wall PhysiologyInner Mitochondrial Membrane ArchitectureIntermembrane Space OrganizationMitochondrial EvolutionMitochondrial Intermembrane Space ProteinsMitochondrial Membrane TopologyOrganelle Membrane OrganizationOuter Mitochondrial Membrane Structure
LACTB is a mammalian active-site serine protein that has evolved from a bacterial penicillin-binding protein. Penicillin-binding proteins are involved in the metabolism of peptidoglycan, the major bacterial cell wall constituent, implying that LACTB has been endowed with novel biochemical properties during eukaryote evolution. Here we demonstrate that LACTB is localized in the mitochondrial intermembrane space, where it is polymerized into stable filaments with a length extending more than a hundred nanometers. We infer that LACTB, through polymerization, promotes intramitochondrial membrane organization and micro-compartmentalization. These findings have implications for our understanding of mitochondrial evolution and function.
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