4YNV

Assembly Chaperone of RpL4 (Acl4) (Residues 28-338)

4YNV の概要

• エントリーDOI: 10.2210/pdb4ynv/pdb
• 関連するPDBエントリー: 4YNW
• 分子名称: ACL4 (1 entity in total)
• 機能のキーワード: ribosome assembly, chaperone, nucleocytoplasmic transport, tetratricopeptide repeat, ribosome biogenesis
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70617.60

構造登録者

Huber, F.M.,Hoelz, A. (登録日: 2015-03-11, 公開日: 2015-05-13, 最終更新日: 2024-11-20)

主引用文献

Stelter, P.,Huber, F.M.,Kunze, R.,Flemming, D.,Hoelz, A.,Hurt, E.
Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension.
Mol.Cell, 58:854-862, 2015

PubMed Abstract: Eukaryotic ribosome biogenesis requires nuclear import and hierarchical incorporation of ∼80 ribosomal proteins (RPs) into the ribosomal RNA core. In contrast to prokaryotes, many eukaryotic RPs possess long extensions that interdigitate in the mature ribosome. RpL4 is a prime example, with an ∼80-residue-long surface extension of unknown function. Here, we identify assembly chaperone Acl4 that initially binds the universally conserved internal loop of newly synthesized RpL4 via its superhelical TPR domain, thereby restricting RpL4 loop insertion at its cognate nascent rRNA site. RpL4 release from Acl4 is orchestrated with pre-ribosome assembly, during which the eukaryote-specific RpL4 extension makes several distinct interactions with the 60S surface, including a co-evolved site on neighboring RpL18. Consequently, mutational inactivation of this contact site, on either RpL4 or RpL18, impairs RpL4-Acl4 disassembly and RpL4 pre-ribosome incorporation. We propose that hierarchical ribosome assembly can be achieved by eukaryotic RP extensions and dedicated assembly chaperones.

PubMed: 25936803
DOI: 10.1016/j.molcel.2015.03.029

実験手法

X-RAY DIFFRACTION (2.95 Å)