• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

Mitochondrial protein import: recognition of internal import signals of BCS1 by the TOM complex.

BCS1, a component of the inner membrane of mitochondria, belongs to the group of proteins with internal, noncleavable import signals. Import and intramitochondrial sorting of BCS1 are encoded in the N-terminal 126 amino acid residues. Three sequence elements were identified in this region, namely, the transmembrane domain (amino acid residues 51 to 68), a presequence type helix (residues 69 to 83), and an import auxiliary region (residues 84 to 126). The transmembrane domain is not required for stable binding to the TOM complex. The Tom receptors (Tom70, Tom22 and Tom20), as determined by peptide scan analysis, interact with the presequence-like helix, yet the highest binding was to the third sequence element. We propose that the initial recognition of BCS1 precursor at the surface of the organelle mainly depends on the auxiliary region and does not require the transmembrane domain. This essential region represents a novel type of signal with targeting and sorting functions. It is recognized by all three known mitochondrial import receptors, demonstrating their capacity to decode various targeting signals. We suggest that the BCS1 precursor crosses the TOM complex as a loop structure and that once the precursor emerges from the TOM complex, all three structural elements are essential for the intramitochondrial sorting to the inner membrane.

Pubmed ID: 12640110

Authors

  • Stan T
  • Brix J
  • Schneider-Mergener J
  • Pfanner N
  • Neupert W
  • Rapaport D

Journal

Molecular and cellular biology

Publication Data

April 17, 2003

Associated Grants

None

Mesh Terms

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Fungal Proteins
  • Macromolecular Substances
  • Membrane Proteins
  • Membrane Transport Proteins
  • Mice
  • Mitochondria
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • Molecular Chaperones
  • Mutagenesis, Site-Directed
  • Neurospora crassa
  • Peptide Library
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Protein Transport
  • Receptors, Cell Surface
  • Receptors, Cytoplasmic and Nuclear
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Structure-Activity Relationship
  • Tetrahydrofolate Dehydrogenase