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In eukaryotes, proteins enter the secretory pathway through the translocon pore of the endoplasmic reticulum. This protein translocation channel is composed of three major subunits, called Sec61α, β and γ in mammals. Unlike the other subunits, the β subunit is dispensable for translocation and cell viability in all organisms studied. Intriguingly, the knockout of the Sec61β encoding genes results in different phenotypes in different species. Nevertheless, the β subunit shows a high level of sequence homology across species, suggesting the conservation of a biological function that remains ill-defined. To address its cellular roles, we characterized the homolog of Sec61β in the fission yeast  Schizosaccharomyces pombe  (Sbh1p). Here, we show that the knockout of  sbh1   +  results in severe cold sensitivity, increased sensitivity to cell-wall stress, and reduced protein secretion at 23°C. Sec61β homologs from  Saccharomyces cerevisiae  and human complement the knockout of  sbh1   +  in  S. pombe . As in  S. cerevisiae , the transmembrane domain (TMD) of  S. pombe  Sec61β is sufficient to complement the phenotypes resulting from the knockout of the entire encoding gene. Remarkably, the TMD of Sec61β from  S. cerevisiae  and human also complement the gene knockouts in both yeasts. Together, these observations indicate that the TMD of Sec61β exerts a cellular function that is conserved across species.

Inter-Species Complementation of the Translocon Beta Subunit Requires Only Its Transmembrane Domain