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Evolutionary conservation of components of the protein translocation complex

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Abstract

PROTEIN translocation into the mammalian endoplasmic reticulum requires the Sec61p complex, which consists of three membrane proteins1. The α-subunit, the homologue of Sec61p of yeast2–4, shows some similarity to SecYp5, a key component of the protein export apparatus of bacteria6,7. In Escherichia coli, SecYp is also associated with two other proteins (SecEp and band-1 protein)8,9. We have now determined the sequences of the β- and γ-subunits of the mammalian Sec61p complex. Sec61-γ is homologous to SSSlp, a suppressor of sec61 mutants in Saccharomyces cerevisiae, and can functionally replace it in yeast cells. Moreover, Sec61-γ and SSSlp are structurally related to SecEp of E. coli and to putative homologues in various other bacteria. At least two sub-units of the Sec61/SecYp complex therefore seem to be key components of the protein translocation apparatus in all classes of organisms.

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Author notes

  1. Dirk Görlich

    Present address: Wellcome/CRC Institute, Tennis Court Road, Cambridge, CB2 1QR, UK

  2. Siegfried Prehn: Institute for Biochemistry, Humboldt-University Berlin, Hessische Strasse 3-4, 10115 Berlin, Germany

  3. Stefan Jentsch: ZMBH, Center for Molecular Biology, University Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany

Authors and Affiliations

  1. Max-Delbrück Centre for Molecular Medicine, Robert-Rössle Strasse 10, 12135, Berlin-Buch, Germany

    Enno Hartmann, Thomas Sommer, Siegfried Prehn, Dirk Görlich, Stefan Jentsch & Tom A. Rapoport

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  1. Enno Hartmann
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  2. Thomas Sommer
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  6. Tom A. Rapoport
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Hartmann, E., Sommer, T., Prehn, S. et al. Evolutionary conservation of components of the protein translocation complex. Nature 367, 654–657 (1994). https://doi.org/10.1038/367654a0

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