LACTB is a filament-forming protein localized in mitochondria

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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2009-11, Vol.106 (45), p.18960-18965
Main Authors: Polianskyte, Zydrune, Peitsaro, Nina, Dapkunas, Arvydas, Liobikas, Julius, Soliymani, Rabah, Lalowski, Maciej, Speer, Oliver, Seitsonen, Jani, Butcher, Sarah, Cereghetti, Grazia M, Linder, Matts D, Merckel, Michael, Thompson, James, Eriksson, Ove
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antibodies
beta-Lactamases - genetics
beta-Lactamases - metabolism
Binding sites
Biochemistry
Biological Sciences
Cell walls
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Eukaryotic cells
Evolution
Filaments
Gels
HeLa Cells
Humans
Immunoblotting
Male
Mammals
Mass Spectrometry
Medicin och hälsovetenskap
Membrane Proteins - genetics
Membrane Proteins - metabolism
Metabolism
Microscopy, Electron, Transmission
Microscopy, Fluorescence
Mitochondria
Mitochondria - metabolism
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Models, Molecular
Molecular Sequence Data
Penicillin
penicillin-binding protein
Penicillin-Binding Proteins - metabolism
peptidoglycans
Plasmids - genetics
Polymerization
Polymers
Polymers - metabolism
Proteins
Rats
Rats, Wistar
Serine
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Summary: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.
ISSN:0027-8424
1091-6490
1091-6490
DOI:10.1073/pnas.0906734106