Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae

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 t wo other proteins, Spc1p and Spc2p, whose functions are largely unknown. Us ing anti-Spc2p antibodies, we show here that this heterotetrameric complex associates with Sbh1p and Sbh2p, the beta -subunits of the Sec61p complex a nd the Ssh1p complex respectively. Depletion of Spc2p decreased the enzymat ic 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 Sbh2 p. These data implicate that Spc2p not only enhances the enzymatic activity of the SPC but also facilitates the interactions between different compone nts of the translocation site.