Interactions between Spc2p and Other Components of the Endoplasmic Reticulum Translocation Sites of the YeastSaccharomyces cerevisiae
| Autor: | H E Meyer, Wolfram Antonin, Enno Hartmann |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Signal peptide
Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Chromosomal translocation Biology Endoplasmic Reticulum Biochemistry Fungal Proteins 03 medical and health sciences 0302 clinical medicine Molecular Biology DNA Primers 030304 developmental biology 0303 health sciences Base Sequence Endoplasmic reticulum STIM1 Cell Biology biology.organism_classification Yeast 3. Good health Cell biology Membrane protein Mutagenesis Microsome 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 275:34068-34072 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m006126200 |
| Popis: | In yeast, the endoplasmic reticulum membrane proteins Sec11p and Spc3p are essential for the cleavage of signal peptides of nascent polypeptide chains during their passage through translocation sites. Genetic and biochemical experiments demonstrate that Sec11p and Spc3p are tightly associated with two other proteins, Spc1p and Spc2p, whose functions are largely unknown. Using anti-Spc2p antibodies, we show here that this heterotetrameric complex associates with Sbh1p and Sbh2p, the beta-subunits of the Sec61p complex and the Ssh1p complex, respectively. Depletion of Spc2p decreased the enzymatic activity of the SPC in vitro, led to a loss of Spc1p, and led to a down-regulation of the amount of Sec11p and Spc3p in the endoplasmic reticulum. Moreover, the deletion of Spc2p also decreased the expression level of Sbh2p. These data implicate that Spc2p not only enhances the enzymatic activity of the SPC but also facilitates the interactions between different components of the translocation site. |
| Databáze: | OpenAIRE |
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