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- W3176544470 abstract "Mitochondria originated from a symbiosis between aerobic bacteria and a pro-eukaryotic cell. After endosymbiosis the molecular machinery for peptidoglycan synthesis was abolished. LACTB (60 kDa) is a mammalian serine protease sharing sequence similarity to proteins involved in peptidoglycan synthesis. A phylogenetic analysis showed that LACTB is most closely related to low molecular weight penicillin-binding proteins class B. Here we have investigated the expression and subcellular location of LACTB. RNA hybridization showed highest expression in brain, heart, skeletal muscle, liver, and kidney. Tissue fractionation, histochemical staining, and immuno EM showed that LACTB is located in the mitochondrial intermembrane space. Native gel electrophoresis showed that LACTB migrates at an apparent molecular weight of 600 kDa, suggesting that LACTB is part of a larger complex. MALDI TOF mass spectrometry of putative of LACTB binding partners identified several proteins involved in metabolism. We could not detect components of the mitochondrial ribosome, suggesting that the assignment of LACTB as a mitoribosomal protein might require further investigation. We conclude that LACTB is a mitochondrial intermembrane space protein that has evolved from penicillin-binding proteins present in the bacterial periplasmic space. The physiological role of LACTB remains to be elucidated." @default.
- W3176544470 created "2021-07-05" @default.
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- W3176544470 date "2006-03-01" @default.
- W3176544470 modified "2023-09-27" @default.
- W3176544470 title "The mammalian serine protease LACTB is located in the mitochondrial intermembrane compartment" @default.
- W3176544470 doi "https://doi.org/10.1096/fasebj.20.4.a495-b" @default.
- W3176544470 hasPublicationYear "2006" @default.
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