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TitleStructural insight into precursor tRNA processing by yeast ribonuclease P.
Journal, issue, pagesScience, Vol. 362, Issue 6415, Year 2018
Publish dateNov 9, 2018
AuthorsPengfei Lan / Ming Tan / Yuebin Zhang / Shuangshuang Niu / Juan Chen / Shaohua Shi / Shuwan Qiu / Xuejuan Wang / Xiangda Peng / Gang Cai / Hong Cheng / Jian Wu / Guohui Li / Ming Lei /
PubMed AbstractRibonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of ...Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures of RNase P alone and in complex with pre-tRNA The protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a "measuring device" with two fixed anchors that recognize the L-shaped pre-tRNA. A universally conserved uridine nucleobase and phosphate backbone in the catalytic center together with the scissile phosphate and the O3' leaving group of pre-tRNA jointly coordinate two catalytic magnesium ions. Binding of pre-tRNA induces a conformational change in the catalytic center that is required for catalysis. Moreover, simulation analysis suggests a two-metal-ion S2 reaction pathway of pre-tRNA cleavage. These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5'-leader of pre-tRNA is processed by eukaryotic RNase P.
External linksScience / PubMed:30262633
MethodsEM (single particle)
Resolution3.48 Å
Structure data

9616

6agb

EMDB-9616, PDB-6agb:
Cryo-EM structure of yeast Ribonuclease P
Method: EM (single particle) / Resolution: 3.48 Å

9622

6ah3

EMDB-9622, PDB-6ah3:
Cryo-EM structure of yeast Ribonuclease P with pre-tRNA substrate
Method: EM (single particle) / Resolution: 3.48 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • Baker's yeast (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsHYDROLASE/RNA / Ribonuclease P / RNA-protein complex / HYDROLASE-RNA complex

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