6XU7

Drosophila melanogaster Testis polysome ribosome

これはPDB形式変換不可エントリーです。

6XU7 の概要

• エントリーDOI: 10.2210/pdb6xu7/pdb
• EMDBエントリー: 10623
• 分子名称: 40S ribosomal protein SA, 40S ribosomal protein S23, 40S ribosomal protein S12, ... (83 entities in total)
• 機能のキーワード: specialised ribosome, drosophila melanogaster, testis, ribosome
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 83
• 化学式量合計: 3388109.55

構造登録者

Hopes, T.,Agapiou, M.,Norris, K.,McCarthy, C.G.P.,OConnell, M.J.,Fontana, J.,Aspden, J.L. (登録日: 2020-01-17, 公開日: 2021-07-28, 最終更新日: 2024-10-23)

主引用文献

Hopes, T.,Norris, K.,Agapiou, M.,McCarthy, C.G.P.,Lewis, P.A.,O'Connell, M.J.,Fontana, J.,Aspden, J.L.
Ribosome heterogeneity in Drosophila melanogaster gonads through paralog-switching.
Nucleic Acids Res., 50:2240-2257, 2022

PubMed Abstract: Ribosomes have long been thought of as homogeneous macromolecular machines, but recent evidence suggests they are heterogeneous and could be specialised to regulate translation. Here, we have characterised ribosomal protein heterogeneity across 4 tissues of Drosophila melanogaster. We find that testes and ovaries contain the most heterogeneous ribosome populations, which occurs through a combination of paralog-enrichment and paralog-switching. We have solved structures of ribosomes purified from in vivo tissues by cryo-EM, revealing differences in precise ribosomal arrangement for testis and ovary 80S ribosomes. Differences in the amino acid composition of paralog pairs and their localisation on the ribosome exterior indicate paralog-switching could alter the ribosome surface, enabling different proteins to regulate translation. One testis-specific paralog-switching pair is also found in humans, suggesting this is a conserved site of ribosome heterogeneity. Overall, this work allows us to propose that mRNA translation might be regulated in the gonads through ribosome heterogeneity, providing a potential means of ribosome specialisation.

PubMed: 34283226
DOI: 10.1093/nar/gkab606

実験手法

ELECTRON MICROSCOPY (4.9 Å)