8J60
Structural and mechanistic insight into ribosomal ITS2 RNA processing by nuclease-kinase machinery
8J60 の概要
エントリーDOI | 10.2210/pdb8j60/pdb |
EMDBエントリー | 33735 |
分子名称 | Polynucleotide 5'-hydroxyl-kinase GRC3, LAS1 protein (2 entities in total) |
機能のキーワード | endoribonuclease; ribosome biosynthesis; las1; grc3, rna binding protein |
由来する生物種 | Cyberlindnera jadinii 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 238052.98 |
構造登録者 | |
主引用文献 | Chen, J.,Chen, H.,Li, S.,Lin, X.,Hu, R.,Zhang, K.,Liu, L. Structural and mechanistic insights into ribosomal ITS2 RNA processing by nuclease-kinase machinery. Elife, 12:-, 2024 Cited by PubMed Abstract: Precursor ribosomal RNA (pre-rRNA) processing is a key step in ribosome biosynthesis and involves numerous RNases. A HEPN (higher eukaryote and prokaryote nucleotide binding) nuclease Las1 and a polynucleotide kinase Grc3 assemble into a tetramerase responsible for rRNA maturation. Here, we report the structures of full-length and Las1-Grc3 complexes, and Las1. The Las1-Grc3 structures show that the central coiled-coil domain of Las1 facilitates pre-rRNA binding and cleavage, while the Grc3 C-terminal loop motif directly binds to the HEPN active center of Las1 and regulates pre-rRNA cleavage. Structural comparison between Las1 and Las1-Grc3 complex exhibits that Grc3 binding induces conformational rearrangements of catalytic residues associated with HEPN nuclease activation. Biochemical assays identify that Las1 processes pre-rRNA at the two specific sites (C2 and C2'), which greatly facilitates rRNA maturation. Our structures and specific pre-rRNA cleavage findings provide crucial insights into the mechanism and pathway of pre-rRNA processing in ribosome biosynthesis. PubMed: 38180340DOI: 10.7554/eLife.86847 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.39 Å) |
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