8K4E

Cryo-EM structure of 30S ribosome with cleaved AP-mRNA bound complex-II

8K4E の概要

• エントリーDOI: 10.2210/pdb8k4e/pdb
• EMDBエントリー: 36883 36885 36886
• 分子名称: AP-mRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (22 entities in total)
• 機能のキーワード: 30s ribosome, ap-mrna, ribosome
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 816336.13

構造登録者

Ramachandran, R.,Afsar, M.,Shukla, A. (登録日: 2023-07-18, 公開日: 2024-07-24, 最終更新日: 2025-01-08)

主引用文献

Afsar, M.,Shukla, A.,Ali, F.,Maurya, R.K.,Bharti, S.,Kumar, N.,Sadik, M.,Chandra, S.,Rahil, H.,Kumar, S.,Ansari, I.,Jahan, F.,Habib, S.,Hussain, T.,Krishnan, M.Y.,Ramachandran, R.
Bacterial Rps3 counters oxidative and UV stress by recognizing and processing AP-sites on mRNA via a novel mechanism.
Nucleic Acids Res., 52:13996-14012, 2024

PubMed Abstract: Lesions and stable secondary structures in mRNA severely impact the translation efficiency, causing ribosome stalling and collisions. Prokaryotic ribosomal proteins Rps3, Rps4 and Rps5, located in the mRNA entry tunnel, form the mRNA helicase center and unwind stable mRNA secondary structures during translation. However, the mechanism underlying the detection of lesions on translating mRNA is unclear. We used Cryo-EM, biochemical assays, and knockdown experiments to investigate the apurinic/apyrimidinic (AP) endoribonuclease activity of bacterial ribosomes on AP-site containing mRNA. Our biochemical assays show that Rps3, specifically the 130RR131 motif, is important for recognizing and performing the AP-endoribonuclease activity. Furthermore, structural analysis revealed cleaved mRNA product in the 30S ribosome entry tunnel. Additionally, knockdown studies in Mycobacterium tuberculosis confirmed the protective role of Rps3 against oxidative and UV stress. Overall, our results show that prokaryotic Rps3 recognizes and processes AP-sites on mRNA via a novel mechanism that is distinct from eukaryotes.

PubMed: 39588766
DOI: 10.1093/nar/gkae1130

実験手法

ELECTRON MICROSCOPY (3.4 Å)