| Literature DB >> 19858488 |
Zydrune Polianskyte1, Nina Peitsaro, Arvydas Dapkunas, Julius Liobikas, Rabah Soliymani, Maciej Lalowski, Oliver Speer, Jani Seitsonen, Sarah Butcher, Grazia M Cereghetti, Matts D Linder, Michael Merckel, James Thompson, Ove Eriksson.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19858488 PMCID: PMC2767363 DOI: 10.1073/pnas.0906734106
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205