| Standard Name | IMP2 1 (see Nomenclature conflict Note) |
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| Systematic Name | YMR035W |
| Feature Type | ORF, Verified |
| Description | Catalytic subunit of the mitochondrial inner membrane peptidase complex, required for maturation of mitochondrial proteins of the intermembrane space; complex contains Imp1p and Imp2p (both catalytic subunits), and Som1p (1, 2 and see Summary Paragraph) |
| Name Description | Inner Membrane Protease 1 |
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| View Computational GO annotations for IMP2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| 40 total interaction(s) for 39 unique genes/features. | |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000004638 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| INM2 | Nomenclature conflict | The gene name IMP2 has been used to refer to the transcriptional coactivator IMP2'/YIL154C, the inositol monophosphatase INM2/YDR287W, and the mitochondrial inner membrane peptidase IMP2/YMR035W. |
| IMP2' | Nomenclature conflict | The gene name IMP2 has been used to refer to the transcriptional coactivator IMP2'/YIL154C, the inositol monophosphatase INM2/YDR287W, and the mitochondrial inner membrane peptidase IMP2/YMR035W. |
About mitochondrial import
While the mitochondrial genome encodes a handful of proteins, most of the hundreds of proteins that reside in the mitochondrion are encoded by nuclear genes, translated in the cytoplasm, and imported into mitochondria via a series of complex molecular machines (see 3, 4 for review). Many of the proteins imported into mitochondria are involved in respiration, which is not an essential process: S. cerevisiae is able to carry out either fermentative growth on carbon sources such as glucose, or respiratory growth on nonfermentable carbon sources such as glycerol and ethanol. However, since maintenance of the mitochondrial compartment is essential to life, mutations that completely disrupt mitochondrial import are lethal.
About the Inner Membrane Protease (IMP)
Most proteins undergo proteolytic processing upon import into mitochondria, and multiple proteases cleave different subsets of these proteins. The Inner Membrane Protease, IMP, processes some proteins that are translocated from the mitochondrial matrix into the intermembrane space. IMP consists of three subunits: Imp1p, Imp2p, and Som1p (2). Both Imp1p and Imp2p are catalytic subunits and share 25% identity, though each protein has distinct substrate specificities (1, 5, 6). Among the substrates of Imp1p are the precursors to NADH-cytochrome b5 reductase (Mcr1p), cytochrome b2 (Cyb2p), FAD-dependent glycerol-3-phosphate dehydrogenase (Gut2p), and the mitochondrially encoded subunit II of cytochrome c oxidase (Cox2p), while the only known substrate of Imp2p is cytochrome c1 (Cyt1p; 2, 7, 1, 8). In addition to its catalytic activity, Imp2p is also required for the stable expression of Imp1p (1). Som1p is a noncatalytic subunit that has been proposed to have a role in substrate recognition and correct functioning of Imp1p; it is required for processing of Cox2p and Mcr1p, and the som1 mutation reduces processing of Cyb2p (2).
Note: another yeast gene has also been referred to as IMP2. This gene is designated as IMP2' in SGD; IMP2' (ORF YIL154C) is a transcription factor involved in maltose, galatose, and raffinose metabolism.
| 1) | Nunnari J, et al. (1993) A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262(5142):1997-2004 |
| 2) | Jan PS, et al. (2000) Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2. Mol Gen Genet 263(3):483-91 |
| 3) | Neupert W and Herrmann JM (2007) Translocation of proteins into mitochondria. Annu Rev Biochem 76:723-49 |
| 4) | Mokranjac D and Neupert W (2009) Thirty years of protein translocation into mitochondria: unexpectedly complex and still puzzling. Biochim Biophys Acta 1793(1):33-41 |
| 5) | Chen X, et al. (1999) Signal peptides having standard and nonstandard cleavage sites can be processed by Imp1p of the mitochondrial inner membrane protease. J Biol Chem 274(53):37750-4 |
| 6) | Pratje E and Guiard B (1986) One nuclear gene controls the removal of transient pre-sequences from two yeast proteins: one encoded by the nuclear the other by the mitochondrial genome. EMBO J 5(6):1313-7 |
| 7) | Esser K, et al. (1996) SOM 1, a small new gene required for mitochondrial inner membrane peptidase function in Saccharomyces cerevisiae. Mol Gen Genet 252(4):437-45 |
| 8) | Esser K, et al. (2004) The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate. Mol Genet Genomics 271(5):616-26 |





