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PMID:10830167

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Citation

Donzeau, M, Káldi, K, Adam, A, Paschen, S, Wanner, G, Guiard, B, Bauer, MF, Neupert, W and Brunner, M (2000) Tim23 links the inner and outer mitochondrial membranes. Cell 101:401-12

Abstract

Tim23, a key component of the mitochondrial preprotein translocase, is anchored in the inner membrane by its C-terminal domain and exposes an intermediate domain in the intermembrane space that functions as a presequence receptor. We show that the N-terminal domain of Tim23 is exposed on the surface of the outer membrane. The two-membrane-spanning topology of Tim23 is a novel characteristic in membrane biology. By the simultaneous integration into two membranes, Tim23 forms contacts between the outer and inner mitochondrial membranes. Tethering the inner membrane translocase to the outer membrane facilitates the transfer of precursor proteins from the TOM complex to the TIM23 complex and increases the efficiency of protein import.

Links

PubMed

Keywords

Animals; Carrier Proteins/metabolism; Intracellular Membranes/metabolism; Intracellular Membranes/ultrastructure; Membrane Proteins/metabolism; Membrane Transport Proteins; Mitochondria/metabolism; Mitochondria/ultrastructure; Rabbits; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:TIM23

involved_in

GO:0030150: protein import into mitochondrial matrix

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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