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J Biol Chem, Vol. 275, Issue 19, 14550-14557, May 12, 2000
From the Universität Göttingen, Zentrum Biochemie und
Molekulare Zellbiologie, Biochemie II, Heinrich-Düker-Weg 12,
Göttingen 37073, the In yeast, efficient protein transport across the
endoplasmic reticulum (ER) membrane may occur co-translationally or
post-translationally. The latter process is mediated by a membrane
protein complex that consists of the Sec61p complex and the
Sec62p-Sec63p subcomplex. In contrast, in mammalian cells protein
translocation is almost exclusively co-translational. This transport
depends on the Sec61 complex, which is homologous to the yeast Sec61p
complex and has been identified in mammals as a ribosome-bound
pore-forming membrane protein complex. We report here the existence of
ribosome-free mammalian Sec61 complexes that associate with two
ubiquitous proteins of the ER membrane. According to primary sequence
analysis both proteins display homology to the yeast proteins Sec62p
and Sec63p and are therefore named Sec62 and Sec63, respectively. The
probable function of the mammalian Sec61-Sec62-Sec63 complex is
discussed with respect to its abundance in ER membranes, which, in
contrast to yeast ER membranes, apparently lack efficient
post-translational translocation activity.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF100141 and U93239.
Mammalian Sec61 Is Associated with Sec62 and Sec63*
,, Max Delbrück Centrum
für Molekulare Medizin, Robert-Rössle-Strasse 10,
Berlin 13092, and the § Charité der Humboldt
Universität Berlin, Institut für Biochemie, Hessische
Strasse 3-4, Berlin 10115, Germany
*
This work was supported by Deutsche Forschungsgemeinschaft
Grants GA 175/11, SFB 523, and GRK 41/3 (to E. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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