Abstract:
:Many proteins located in the intermembrane space (IMS) of mitochondria are characterized by a low molecular mass, contain highly conserved cysteine residues and coordinate metal ions. Studies on one of these proteins, Tim13, revealed that net translocation across the outer membrane is driven by metal-dependent folding in the IMS . We have identified an essential component, Mia40/Tim40/Ykl195w, with a highly conserved domain in the IMS that is able to bind zinc and copper ions. In cells lacking Mia40, the endogenous levels of Tim13 and other metal-binding IMS proteins are strongly reduced due to the impaired import of these proteins. Furthermore, Mia40 directly interacts with newly imported Tim13 protein. We conclude that Mia40 is the first essential component of a specific translocation pathway of metal-binding IMS proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Terziyska N,Lutz T,Kozany C,Mokranjac D,Mesecke N,Neupert W,Herrmann JM,Hell Kdoi
10.1016/j.febslet.2004.11.072keywords:
subject
Has Abstractpub_date
2005-01-03 00:00:00pages
179-84issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(04)01468-1journal_volume
579pub_type
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