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TitleStructural insights into human ELAC2 as a tRNA 3' processing enzyme.
Journal, issue, pagesNucleic Acids Res, Vol. 52, Issue 21, Page 13434-13446, Year 2024
Publish dateNov 27, 2024
AuthorsChenyang Xue / Junshan Tian / Yanhong Chen / Zhongmin Liu /
PubMed AbstractHuman elaC ribonuclease Z 2 (ELAC2) removes the 3' trailer of precursor transfer ribonucleic acid (pre-tRNA). Mutations in ELAC2 are highly associated with the development of prostate cancer and ...Human elaC ribonuclease Z 2 (ELAC2) removes the 3' trailer of precursor transfer ribonucleic acid (pre-tRNA). Mutations in ELAC2 are highly associated with the development of prostate cancer and hypertrophic cardiomyopathy. However, the catalytic mechanism of ELAC2 remains unclear. We determined the cryogenic electron microscopy structures of human ELAC2 in various states, including the apo, pre-tRNA-bound and tRNA-bound states, which enabled us to identify the structural basis for its binding to pre-tRNA and cleavage of the 3' trailer. Notably, conformational rearrangement of the C-terminal helix was related to feeding of the 3' trailer into the cleavage site, possibly explaining why its mutations are associated with disease. We further used biochemical assays to analyse the structural effects of disease-related mutations of human ELAC2. Collectively, our data provide a comprehensive structural basis for how ELAC2 recruits pre-tRNA via its flexible arm domain and guides the 3' trailer of pre-tRNA into the active centre for cleavage by its C-terminal helix.
External linksNucleic Acids Res / PubMed:39494506 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.3 Å
Structure data

39710

8z0p

EMDB-39710, PDB-8z0p:
Cryo-EM structure of human ELAC2
Method: EM (single particle) / Resolution: 3.1 Å

39726

8z1f

EMDB-39726, PDB-8z1f:
Cryo-EM structure of human ELAC2-tRNA
Method: EM (single particle) / Resolution: 4.3 Å

39727

8z1g

EMDB-39727, PDB-8z1g:
Cryo-EM structure of human ELAC2-pre-tRNA
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / endonuclease Zinc phosphodiesterase

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