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Proper insertion and topogenesis of membrane proteins in the ER depend on Sec63
Cited 11 time in
Web of Science
Cited 11 time in Scopus
- Authors
- Issue Date
- 2019-09
- Publisher
- Elsevier BV
- Citation
- Biochimica et Biophysica Acta - General Subjects, Vol.1863 No.9, pp.1371-1380
- Abstract
- Background: In eukaryotic cells, biogenesis of proteins destined to the secretory pathway begins from the cytosol. Nascent chains are either co-translationally or post-translationally targeted to the endoplasmic reticulum (ER) and translocated across the membrane through the Sec61 complex. For the post-translational translocation, the Sec62/Sec63 complex is additionally required. Sec63, however, is also shown to mediate co-translational translocation of a subset of proteins, the types and characteristics of proteins that Sec63 mediates in translocation still await to be defined. Methods: To overview the types of proteins that require Sec63 for the ER translocation, we prepared Sec63 mutant lacking the first 39 residues (Sec63_Delta N39) in yeast and assessed initial translocation efficiencies of diverse types of precursors in the sec63_Delta N39 strain by a 5 min metabolic labeling. By employing Blue-Native gel electrophoresis (BN-PAGE), stability of the SEC complex (Sec61 plus Sec62/Sec63 complexes) isolated from cells carrying the Sec63_Delta N39 mutant was examined. Results: Among the various translocation precursors tested, we found that proper sorting of single- and double-pass membrane proteins was severely impaired in addition to post-translational translocation precursor in the sec63_Delta N39 mutant strain. Stability of the SEC complex was compromised upon deletion of the N-terminal 39 residues. Conclusions: The N-terminus of Sec63 is important for stability of the SEC complex and Sec63 is required for proper sorting of membrane proteins in vivo. General significance: Sec63 is essential on insertion of membrane proteins.
- ISSN
- 0304-4165
- Language
- ENG
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