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-Structure paper
タイトル | Stabilization of Ribosomal RNA of the Small Subunit by Spermidine in . |
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ジャーナル・号・ページ | Front Mol Biosci, Vol. 8, Page 738752, Year 2021 |
掲載日 | 2021年11月18日 |
著者 | Margarita Belinite / Iskander Khusainov / Heddy Soufari / Stefano Marzi / Pascale Romby / Marat Yusupov / Yaser Hashem / |
PubMed 要旨 | Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution ...Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution structures using this approach, one needs to obtain homogeneous and stable samples, which requires optimization of ribosome purification in a species-dependent manner. This is especially critical for the bacterial small ribosomal subunit that tends to be unstable in the absence of ligands. Here, we report a protocol for purification of stable 30 S from the Gram-positive bacterium and its cryo-EM structures: in presence of spermidine at a resolution ranging between 3.4 and 3.6 Å and in its absence at 5.3 Å. Using biochemical characterization and cryo-EM, we demonstrate the importance of spermidine for stabilization of the 30 S preserving favorable conformation of the helix 44. |
リンク | Front Mol Biosci / PubMed:34869582 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 - 13.76 Å |
構造データ | EMDB-12090: EMDB-12091: EMDB-12178, PDB-7bgd: EMDB-12179, PDB-7bge: EMDB-23052, PDB-7kwg: |
由来 |
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キーワード | RIBOSOME / Pathogen / small ribosomal subunit / spermidine |