The Tom Core Complex
نویسندگان
چکیده
منابع مشابه
The Tom Core Complex
Translocation of nuclear-encoded preproteins across the outer membrane of mitochondria is mediated by the multicomponent transmembrane TOM complex. We have isolated the TOM core complex of Neurospora crassa by removing the receptors Tom70 and Tom20 from the isolated TOM holo complex by treatment with the detergent dodecyl maltoside. It consists of Tom40, Tom22, and the small Tom components, Tom...
متن کاملThe TOM Core Complex: The General Protein Import Pore of the Outer Membrane of Mitochondria
Translocation of nuclear-encoded preproteins across the outer membrane of mitochondria is mediated by the multicomponent transmembrane TOM complex. We have isolated the TOM core complex of Neurospora crassa by removing the receptors Tom70 and Tom20 from the isolated TOM holo complex by treatment with the detergent dodecyl maltoside. It consists of Tom40, Tom22, and the small Tom components, Tom...
متن کاملThe Broken - Circuit Complex 1 by Tom
The broken-circuit complex introduced by H. Wilf (Which polynomials are chromatic!, Proc. Colloq. Combinational Theory (Rome, 1973)) of a matroid G is shown to be a cone over a related complex, the reduced broken-circuit complex Q'(G). The topological structure of Q'(G) is studied, its Euler characteristic is computed, and joins and skeletons are shown to exist in the class of all such complexe...
متن کاملBiogenesis of Tom40, Core Component of the Tom Complex of Mitochondria
Tom40 is an essential component of the preprotein translocase of the mitochondrial outer membrane (TOM complex) in which it constitutes the core element of the protein conducting pore. We have investigated the biogenesis of Tom40. Tom40 is inserted into the outer membrane by the TOM complex. Initially, Tom40 is bound as a monomer at the mitochondrial surface. The import receptor Tom20 is involv...
متن کاملTransport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex.
Members of the mitochondrial carrier family such as the ADP/ATP carrier (AAC) are composed of three structurally related modules. Here we show that each of the modules contains a mitochondrial import signal recognized by Tim10 and Tim12 in the intermembrane space. The first and the second module are translocated across the outer membrane independently of the membrane potential, DeltaDeltapsipsi...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1999
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.147.5.959