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-Structure paper
タイトル | Structural insights into the interplay of protein biogenesis factors with the 70S ribosome. |
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ジャーナル・号・ページ | Structure, Vol. 29, Issue 7, Page 755-767.e4, Year 2021 |
掲載日 | 2021年7月1日 |
著者 | Shirin Akbar / Sayan Bhakta / Jayati Sengupta / |
PubMed 要旨 | Bacterial co-translational N-terminal methionine excision, an early event of nascent polypeptide chain processing, is mediated by two enzymes: peptide deformylase (PDF) and methionine aminopeptidase ...Bacterial co-translational N-terminal methionine excision, an early event of nascent polypeptide chain processing, is mediated by two enzymes: peptide deformylase (PDF) and methionine aminopeptidase (MetAP). Trigger factor (TF), the only ribosome-associated bacterial chaperone, offers co-translational chaperoning assistance. Here, we present two high-resolution cryoelectron microscopy structures of tRNA-bound E. coli ribosome complexes showing simultaneous binding of PDF and TF, in the absence (3.4 Å) and presence of MetAP (4.1 Å). These structures establish molecular details of the interactions of the factors with the ribosome, and thereby reveal the structural basis of nascent chain processing. Our results suggest that simultaneous binding of all three factors is not a functionally favorable mechanism of nascent chain processing. Strikingly, an unusual structural distortion of the 70S ribosome, potentially driven by binding of multiple copies of MetAP, is observed when MetAP is incubated with a pre-formed PDF-TF-bound ribosome complex. |
リンク | Structure / PubMed:33761323 |
手法 | EM (単粒子) |
解像度 | 3.4 - 4.1 Å |
構造データ | EMDB-30598: Cryo-EM structure of 70S ribosome in complex with peptide deformylase and trigger factor EMDB-30611: Cryo-EM map of 70S ribosome in complex with peptide deformylase, trigger factor, and methionine aminopeptidase |
由来 |
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キーワード | RIBOSOME / Escherichia coli / nascent chain / protein biogenesis / peptide deformylase / trigger factor / methionine aminopeptidase |