Literature DB >> 11768763

Signals and receptors--the translocation machinery on the mitochondrial surface.

E Schleiff1.   

Abstract

Most proteins involved in mitochondrial biogenesis are encoded by the genome of the nucleus. They are synthesized in the cytosol and have to be transported toward and, subsequently, imported into the organelle. This targeting and import process is initiated by the specific mitochondrial targeting signal, which differs pending on the final localization of the protein. The preprotein will be recognized by cytosolic proteins, which function in transport toward the mitochondria and in maintaining the import competent state of the preprotein. The precursor will be transferred onto a multicomponent complex on the outer mitochondrial membrane, formed by receptor proteins and the general insertion pore (GIP). Some proteins are directly sorted into the outer membrane whereas the majority will be transported over the outer membrane through the import channel followed by further distribution of those proteins.

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Year:  2000        PMID: 11768763     DOI: 10.1023/a:1005512412404

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN: 0145-479X            Impact factor:   2.945


  124 in total

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Journal:  Trends Biochem Sci       Date:  1991-05       Impact factor: 13.807

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Journal:  J Biol Chem       Date:  1996-10-18       Impact factor: 5.157

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Journal:  Nature       Date:  1990-12-13       Impact factor: 49.962

4.  Mitochondrial import: crossing the aqueous intermembrane space.

Authors:  N Pfanner
Journal:  Curr Biol       Date:  1998-04-09       Impact factor: 10.834

Review 5.  Protein import into mitochondria.

Authors:  W Neupert
Journal:  Annu Rev Biochem       Date:  1997       Impact factor: 23.643

6.  The mitochondrial receptor complex: a central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore.

Authors:  M Kiebler; P Keil; H Schneider; I J van der Klei; N Pfanner; W Neupert
Journal:  Cell       Date:  1993-08-13       Impact factor: 41.582

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Authors:  H Murakami; G Blobel; D Pain
Journal:  Nature       Date:  1990-10-04       Impact factor: 49.962

8.  Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharomyces cerevisiae mitochondria.

Authors:  M Moczko; B Ehmann; F Gärtner; A Hönlinger; E Schäfer; N Pfanner
Journal:  J Biol Chem       Date:  1994-03-25       Impact factor: 5.157

9.  Mitochondrial protein import: involvement of the mature part of a cleavable precursor protein in the binding to receptor sites.

Authors:  N Pfanner; H K Müller; M A Harmey; W Neupert
Journal:  EMBO J       Date:  1987-11       Impact factor: 11.598

10.  Topogenesis of mitochondrial inner membrane uncoupling protein. Rerouting transmembrane segments to the soluble matrix compartment.

Authors:  X Q Liu; A W Bell; K B Freeman; G C Shore
Journal:  J Cell Biol       Date:  1988-08       Impact factor: 10.539

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  4 in total

1.  Chloroplast protein import inhibition by a soluble factor from wheat germ lysate.

Authors:  Enrico Schleiff; Michael Motzkus; Jürgen Soll
Journal:  Plant Mol Biol       Date:  2002-09       Impact factor: 4.076

2.  Cloning and characterization of a 35-kDa mouse mitochondrial outer membrane protein MOM35 with high homology to Tom40.

Authors:  I L Rivera; G C Shore; E Schleiff
Journal:  J Bioenerg Biomembr       Date:  2000-02       Impact factor: 2.945

3.  A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria.

Authors:  Abhijit Mukhopadhyay; Li Ni; Henry Weiner
Journal:  Biochem J       Date:  2004-08-15       Impact factor: 3.857

4.  A novel N-terminal domain may dictate the glucose response of Mondo proteins.

Authors:  Lisa G McFerrin; William R Atchley
Journal:  PLoS One       Date:  2012-04-10       Impact factor: 3.240

  4 in total

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