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-Structure paper
Title | Structural and mechanistic insights into ribosomal ITS2 RNA processing by nuclease-kinase machinery. |
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Journal, issue, pages | Elife, Vol. 12, Year 2024 |
Publish date | Jan 5, 2024 |
![]() | Jiyun Chen / Hong Chen / Shanshan Li / Xiaofeng Lin / Rong Hu / Kaiming Zhang / Liang Liu / ![]() |
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 ...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. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.8 - 3.69 Å |
Structure data | EMDB-33733: Cryo-EM structure of ScLas1-Grc3 complex EMDB-33735: Cryo-EM structure of CjLas1-Grc3 complex ![]() PDB-7y16: ![]() PDB-7y17: ![]() PDB-7y18: |
Chemicals | ![]() ChemComp-HOH: |
Source |
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