The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70
Open accessAbstract
The preprotein translocase of the outer mitochondrial membrane (Tom) is a multi-subunit complex required for specific recognition and membrane translocation of nuclear-encoded preproteins. We have expressed and purified the cytosolic domains of three postulated import receptors, Tom20, Tom22, and Tom70. Each receptor domain is able to bind mitochondrial preproteins but with different specificity. Tom20 binds both preproteins with N-terminal presequences and preproteins with internal targeting signals; the binding is enhanced by the addition of salt. Tom22 selectively recognizes presequence-carrying preproteins in a salt-sensitive manner. Tom70 preferentially binds preproteins with internal targeting information. A chemically synthesized presequence peptide competes with preproteins for binding to Tom20 and Tom22 but not to Tom70. We conclude that each of the three import receptors binds preproteins independently and by a different mechanism. Both Tom20 and Tom22 function as presequence receptors.
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Cites
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MOM19, an import receptor for mitochondrial precursor proteins
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Self-citationPfanner, N., Tropschug, M., & Neupert, W. (1987) · Cell · doi:10.1016/0092-8674(87)90619-2 · Cited by 319
Self-citationA mitochondrial import receptor for the ADP/ATP carrier
Söllner, T., Pfaller, R., Griffiths, G., Pfanner, N., & Neupert, W. (1990) · Cell · doi:10.1016/0092-8674(90)90244-9 · Cited by 297
Self-citationTom5 functionally links mitochondrial preprotein receptors to the general import pore
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Self-citationAmphiphilicity is essential for mitochondrial presequence function.
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Cited by
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915
Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms
Gordon, D. E., Hiatt, J., Bouhaddou, M., Rezelj, V. V., Ulferts, S., Braberg, H., Jureka, A. S., Obernier, K., Guo, J. Z., Batra, J., et al. (2020) · Science · doi:10.1126/science.abe9403 · Cited by 747
Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670
Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
Hill, K., Model, K., Ryan, M. T., Dietmeier, K., Martin, F., Wagner, R., & Pfanner, N. (1998) · Nature · doi:10.1038/26780 · Cited by 512
Self-citationThe Preprotein Translocation Channel of the Outer Membrane of Mitochondria
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Metadata
- Authors
- Brix, J., Dietmeier, K., & Pfanner, N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-08
- Volume
- 272
- Issue
- 33
- Pages
- 20730-20735
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1998397779
- Cited by
- 289
- References
- 37
- FWCI
- 4.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70. https://app.cochat.ai/papers/10.1074/jbc.272.33.20730
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- Brix, J., Dietmeier, K., & Pfanner, N. (1997). Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.33.20730
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