期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 16, 期 6, 页码 589-597出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1614
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资金
- Deutsche Forschungsgemeinschaft (DFG) [SFB 638, FOR967]
- Swiss National Science Foundation (SNSF)
- National Center of Excellence in Research (NCCR)
- SNSF
- ETH Research [TH-3/04-1]
- Federation of European Biochemical Societies
The early events in the life of newly synthesized proteins in the cellular environment are remarkably complex. Concurrently with their synthesis by the ribosome, nascent polypeptides are subjected to enzymatic processing, chaperone-assisted folding or targeting to translocation pores at membranes. The ribosome itself has a key role in these different tasks and governs the interplay between the various factors involved. Indeed, the ribosome serves as a platform for the spatially and temporally regulated association of enzymes, targeting factors and chaperones that act upon the nascent polypeptides emerging from the exit tunnel. Furthermore, the ribosome provides opportunities to coordinate the protein-synthesis activity of its peptidyl transferase center with the protein targeting and folding processes. Here we review the early co-translational events involving the ribosome that guide cytosolic proteins to their native state.
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