Human ABCE1 exhibits temperature-dependent heterologous co-functionality in S. cerevisiae

ABCE1 protein (Rli1 in Saccharomyces cerevisiae) is a unique ribosome recycling factor that is composed of an N-terminal FeS cluster domain and two ATPase domains. Here, we report that heterologous expression of human ABCE1 in S. cerevisiae is unable to complement conditional knockout of ABCE1 (Rli1), at a typical experimental temperature of 30 degrees C. However, low but significant growth was observed at high temperature, 37 degrees C. Considering the close interaction of ABCE1 with translation factors and ribosomal components, the observed temperature-dependent complementation may be attributed to heterologous co-functionality of ABCE1 with S. cerevisiae factor(s), and might reflect functional upregulation of human ABCE1 at its functional temperature.

Automated summary

Heterologous expression of human ABCE1 in S. cerevisiae cannot replace the function of Rli1, but shows low but significant growth at high temperature. This may be attributed to heterologous co-functionality of ABCE1 with S. cerevisiae factor(s) and functional upregulation of human ABCE1 at its functional temperature.