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PMID: 8754801 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.

Molecular and cellular biology ·Vol. 16 ·No. 8 ·1996-08-00 ·Pages 4035-42

Court DA, Nargang FE, Steiner H, Hodges RS, Neupert W, Lill R

Abstract

Tom22 is an essential component of the protein translocation complex (Tom complex) of the mitochondrial outer membrane. The N-terminal domain of Tom22 functions as a preprotein receptor in cooperation with Tom20. The role of the C-terminal domain of Tom22, which is exposed to the intermembrane space (IMS), in its own assembly into the Tom complex and in the import of other preproteins was investigated. The C-terminal domain of Tom22 is not essential for the targeting and assembly of this protein, as constructs lacking part or all of the IMS domain became imported into mitochondria and assembled into the Tom complex. Mutant strains of Neurospora expressing the truncated Tom22 proteins were generated by a novel procedure. These mutants displayed wild-type growth rates, in contrast to cells lacking Tom22, which are not viable. The import of proteins into the outer membrane and the IMS of isolated mutant mitochondria was not affected. Some but not all preproteins destined for the matrix and inner membrane were imported less efficiently. The reduced import was not due to impaired interaction of presequences with their specific binding site on the trans side of the outer membrane. Rather, the IMS domain of Tom22 appears to slightly enhance the efficiency of the transfer of these preproteins to the import machinery of the inner membrane.

MeSH Terms
Base Sequence Biological Transport Cell Compartmentation DNA Primers/chemistry Fungal Proteins/metabolism Membrane Proteins/metabolism,ultrastructure Membrane Transport Proteins Mitochondria/metabolism Molecular Sequence Data Neurospora crassa Protein Precursors/metabolism Receptors, Cell Surface Sequence Deletion Structure-Activity Relationship
Chemicals
DNA Primers Fungal Proteins Membrane Proteins Membrane Transport Proteins Protein Precursors Receptors, Cell Surface
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Court D A
Institut für Physiologische Chemie, Physikalische Biochemie, Zellbiologie der Universität München, Munich, Germany.
Nargang F E
Steiner H
Hodges R S
Neupert W
Lill R
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.16.8.4035
Published
1996-08-00
Pages
4035-42
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC231399
Subset
IM
External Links
PubMed source DOI: 10.1128/MCB.16.8.4035 PMC Full Text View journal details
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