Mam33p, an oligomeric, acidic protein in the mitochondrial matrix of Saccharomyces cerevisiae is related to the human complement receptor gC1q-R
✍ Scribed by Tilman Seytter; Friedrich Lottspeich; Walter Neupert; Elisabeth Schwarz
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 158 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0749-503X
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✦ Synopsis
Mam33p (mitochondrial acidic matrix protein) is a soluble protein, located in mitochondria of Saccharomyces cerevisiae. It is synthesized as a precursor with an N-terminal mitochondrial targeting sequence that is processed on import. Mam33p assembles to a homo-oligomeric complex in the mitochondrial matrix. It can bind to the sorting signal of cytochrome b 2 that directs this protein into the intermembrane space. Mam33p is encoded by an 801 bp open reading frame. Gene disruption did not result in a significant growth defect. Mam33p exhibits sequence similarity to gC1q-R, a human protein that has been implicated in the binding of complement factor C1q and kininogen. 1998