5AOX

Human Alu RNA retrotransposition complex in the ribosome-stalling conformation

5AOX の概要

• エントリーDOI: 10.2210/pdb5aox/pdb
• 分子名称: SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN, SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN, ALU JO CONSENSUS RNA, ... (8 entities in total)
• 機能のキーワード: translation, retrotransposition, protein targeting, rna, mobile dna, sine, line, ribonucleoprotein particle, signal recognition particle
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 98062.62

構造登録者

Ahl, V.,Weichenrieder, O. (登録日: 2015-09-12, 公開日: 2015-11-11, 最終更新日: 2024-01-10)

主引用文献

Ahl, V.,Keller, H.,Schmidt, S.,Weichenrieder, O.
Retrotransposition and Crystal Structure of an Alu Rnp in the Ribosome-Stalling Conformation.
Mol.Cell, 60:715-, 2015

PubMed Abstract: The Alu element is the most successful human genomic parasite affecting development and causing disease. It originated as a retrotransposon during early primate evolution of the gene encoding the signal recognition particle (SRP) RNA. We defined a minimal Alu RNA sufficient for effective retrotransposition and determined a high-resolution structure of its complex with the SRP9/14 proteins. The RNA adopts a compact, closed conformation that matches the envelope of the SRP Alu domain in the ribosomal translation elongation factor-binding site. Conserved structural elements in SRP RNAs support an ancient function of the closed conformation that predates SRP9/14. Structure-based mutagenesis shows that retrotransposition requires the closed conformation of the Alu ribonucleoprotein particle and is consistent with the recognition of stalled ribosomes. We propose that ribosome stalling is a common cause for the cis-preference of the mammalian L1 retrotransposon and for the efficiency of the Alu RNA in hijacking nascent L1 reverse transcriptase.

PubMed: 26585389
DOI: 10.1016/J.MOLCEL.2015.10.003

実験手法

X-RAY DIFFRACTION (2.04 Å)