TY - JOUR
T1 - Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans
AU - Müller, Linda
AU - De Escauriaza, Maria Diaz
AU - Lajoie, Patrick
AU - Theis, Melanie
AU - Jung, Martin
AU - Müller, Anika
AU - Burgard, Carsten
AU - Greiner, Markus
AU - Snapp, Erik L.
AU - Dudek, Johanna
AU - Zimmermann, Richard
PY - 2010/3/1
Y1 - 2010/3/1
N2 - Because of similarity to their yeast orthologues, the two membrane proteins of the human endoplasmic reticulum (ER) Sec62 and Sec63 are expected to play a role in protein biogenesis in the ER. We characterized interactions between these two proteins as well as the putative interaction of Sec62 with ribosomes. These data provide further evidence for evolutionary conservation of Sec62/Sec63 interaction. In addition, they indicate that in the course of evolution Sec62 of vertebrates has gained an additional function, the ability to interact with the ribosomal tunnel exit and, therefore, to support cotranslational mechanisms such as protein transport into the ER. This view is supported by the observation that Sec62 is associated with ribosomes in human cells. Thus, the human Sec62/Sec63 complex and the human ER membrane protein ERj1 are similar in providing binding sites for BiP in the ER-lumen and binding sites for ribosomes in the cytosol. We propose that these two systems provide similar chaperone functions with respect to different precursor proteins.
AB - Because of similarity to their yeast orthologues, the two membrane proteins of the human endoplasmic reticulum (ER) Sec62 and Sec63 are expected to play a role in protein biogenesis in the ER. We characterized interactions between these two proteins as well as the putative interaction of Sec62 with ribosomes. These data provide further evidence for evolutionary conservation of Sec62/Sec63 interaction. In addition, they indicate that in the course of evolution Sec62 of vertebrates has gained an additional function, the ability to interact with the ribosomal tunnel exit and, therefore, to support cotranslational mechanisms such as protein transport into the ER. This view is supported by the observation that Sec62 is associated with ribosomes in human cells. Thus, the human Sec62/Sec63 complex and the human ER membrane protein ERj1 are similar in providing binding sites for BiP in the ER-lumen and binding sites for ribosomes in the cytosol. We propose that these two systems provide similar chaperone functions with respect to different precursor proteins.
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U2 - 10.1091/mbc.E09-08-0730
DO - 10.1091/mbc.E09-08-0730
M3 - Article
C2 - 20071467
AN - SCOPUS:77649164867
SN - 1059-1524
VL - 21
SP - 691
EP - 703
JO - Molecular biology of the cell
JF - Molecular biology of the cell
IS - 5
ER -