TIM/TOM complex
| mitochondrial protein-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.4.2.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The TIM/TOM complex is a protein complex in cellular biochemistry which translocates proteins produced from nuclear DNA through the mitochondrial membrane for use in oxidative phosphorylation. In enzymology, the complex is described as an mitochondrial protein-transporting ATPase (EC 7.4.2.3), or more systematically ATP phosphohydrolase (mitochondrial protein-importing), as the TIM part requires ATP hydrolysis to work.
Only 13 proteins necessary for a mitochondrion are actually coded in mitochondrial DNA. The vast majority of proteins destined for the mitochondria are encoded in the nucleus and synthesised in the cytoplasm. These are tagged by an N-terminal or/and a C-terminal signal sequence. Following transport through the cytosol from the nucleus, the signal sequence is recognized by a receptor protein in the translocase of the outer membrane (TOM) complex. The signal sequence and adjacent portions of the polypeptide chain are inserted in the TOM complex, then begin interaction with a translocase of the inner membrane (TIM) complex, which are hypothesized to be transiently linked at sites of close contact between the two membranes. The signal sequence is then translocated into the matrix in a process that requires an electrochemical hydrogen ion gradient across the inner membrane. Mitochondrial Hsp70 binds to regions of the polypeptide chain and maintains it in an unfolded state as it moves into the matrix.[1]
The ATPase domain is essential during the interactions of the proteins Hsp70 and subunit Tim44.[2] Without the presence of ATPase, carboxy-terminal segment is not able to bind to protein of Tim44.[2] As mtHsp70 transmits the nucleotide state of the ATPase domain with alpha-helices A and B, Tim44 interacts with the peptide binding domain to coordinate the protein bind.[3]
TIC/TOC Complex vs. TIM/TOM Complex
[edit]This protein complex is functionally analogous to the TIC/TOC complex located on the inner and outer membranes of the chloroplast, in the sense that it transports proteins into the membrane of the mitochondria. Although they both hydrolyze triphosphates, they are evolutionally unrelated.[4]
References
[edit]- ^ B. Alberts, A. Johnson, J. Lewis, M. Raff,. K. Roberts, P. Walter. Molecular Biology of the Cell
- ^ a b Krimmer, T.; Rassow, J.; Kunau, W. H.; Voos, W.; Pfanner, N. (2000-08-01). "Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role". Molecular and Cellular Biology. 20 (16): 5879–5887. doi:10.1128/mcb.20.16.5879-5887.2000. ISSN 0270-7306. PMC 86065. PMID 10913171.
- ^ Moro, Fernando; Okamoto, Koji; Donzeau, Mariel; Neupert, Walter; Brunner, Michael (2002-03-01). "Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44". The Journal of Biological Chemistry. 277 (9): 6874–6880. doi:10.1074/jbc.M107935200. ISSN 0021-9258. PMID 11733493.
- ^ P. Jarvis, J. Soll, Toc, Tic and chloroplast protein import
- Bömer U, Meijer M, Maarse AC, Hönlinger A, Dekker PJ, Pfanner N, Rassow J (May 1997). "Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane". The EMBO Journal. 16 (9): 2205–16. doi:10.1093/emboj/16.9.2205. PMC 1169823. PMID 9171336.
- Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W, Brunner M (June 1995). "The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system". Cell. 81 (7): 1085–93. doi:10.1016/S0092-8674(05)80013-3. PMID 7600576.
- Voos W, Martin H, Krimmer T, Pfanner N (November 1999). "Mechanisms of protein translocation into mitochondria". Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes. 1422 (3): 235–54. doi:10.1016/s0304-4157(99)00007-6. PMID 10548718.
External links
[edit]- TCDB 3.A.8 - description of the entire complex
- Overview of the various import ways into mitochondria (group of N. Pfanner)
- [1]
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