期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 42, 页码 16516-16521出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0704664104
关键词
cotranslational folding
资金
- MRC [MC_U117533887] Funding Source: UKRI
- Medical Research Council [MC_U117533887] Funding Source: researchfish
- Medical Research Council [MC_U117533887] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Protein folding in living cells is inherently coupled to protein synthesis and chain elongation. There is considerable evidence that some nascent chains fold into their native structures in a cotranslational manner before release from the ribosome, but, despite its importance, a detailed description of such a process at the atomic level remains elusive. We show here at a residue-specific level that a nascent protein chain can reach its native tertiary structure on the ribosome. By generating translation-arrested ribosomes in which the newly synthesized polypepticle chain is selectively C-13/N-15-labeled, we observe, using ultrafast NMR techniques, a large number of resonances of a ribosome-bound nascent chain complex corresponding to a pair of C-terminally truncated immunoglobulin (1g) domains. Analysis of these spectra reveals that the nascent chain adopts a structure in which a native-like N-tdrminal Ig domain is tethered to the ribosome by a largely unfolded and highly flexible C-terminal domain. Selective broadening of resonances for a group of residues that are colocalized in the structure demonstrates that there are specific but transient interactions between the ribosome and the N-terminal region of the folded Ig domain. These findings represent a step toward a detailed structural understanding of the cellular processes of cotranslational folding.
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