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-Structure paper
タイトル | Cysteine oxidation and disulfide formation in the ribosomal exit tunnel. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 5569, Year 2020 |
掲載日 | 2020年11月4日 |
著者 | Linda Schulte / Jiafei Mao / Julian Reitz / Sridhar Sreeramulu / Denis Kudlinzki / Victor-Valentin Hodirnau / Jakob Meier-Credo / Krishna Saxena / Florian Buhr / Julian D Langer / Martin Blackledge / Achilleas S Frangakis / Clemens Glaubitz / Harald Schwalbe / |
PubMed 要旨 | Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide ...Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive. Here, we investigate the eye-lens protein γB-crystallin in the ribosomal exit tunnel. Using mass spectrometry, theoretical simulations, dynamic nuclear polarization-enhanced solid-state nuclear magnetic resonance and cryo-electron microscopy, we show that thiol groups of cysteine residues undergo S-glutathionylation and S-nitrosylation and form non-native disulfide bonds. Thus, covalent modification chemistry occurs already prior to nascent chain release as the ribosome exit tunnel provides sufficient space even for disulfide bond formation which can guide protein folding. |
リンク | Nat Commun / PubMed:33149120 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.58 - 2.83 Å |
構造データ | EMDB-10891, PDB-6ys3: |
由来 |
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キーワード | RIBOSOME / Translation / 50S ribosome / Nascent peptide chain / translation 50S ribosome nascent peptide chain |