Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit |
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| Authors: | Xueqiang Zhao and Jussi J?ntti |
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| Institution: | (1) Research Program in Cell and Molecular Biology, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Helsinki, 00014, Finland;(2) The State Key Laboratory of Plant Cell and Chromosomal Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, PR, China |
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| Abstract: | Background In eukaryotic cells co- and post-translational protein translocation is mediated by the trimeric Sec61 complex. Currently,
the role of the Sec61 complex β-subunit in protein translocation is poorly understood. We have shown previously that in Saccharomyces cerevisiae the trans-membrane domain alone is sufficient for the function of the β-subunit Sbh1p in co-translational protein translocation.
In addition, Sbh1p co-purifies not only with the protein translocation channel subunits Sec61p and Sss1p, but also with the
reticulon family protein Rtn1p. |
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