Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions.

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 Lett

journal_title

FEBS letters

authors

Terziyska N,Lutz T,Kozany C,Mokranjac D,Mesecke N,Neupert W,Herrmann JM,Hell K

doi

10.1016/j.febslet.2004.11.072

keywords:

subject

Has Abstract

pub_date

2005-01-03 00:00:00

pages

179-84

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(04)01468-1

journal_volume

579

pub_type

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