The Thunder team revealed the processing maturity mechanism at the tRNA precursor 5' end of eyre.

The Thunder team at the Institute of Precision Medicine of the Ninth People's Hospital, affiliated with Shanghai Jiaotong University School of Medicine, revealed the processing maturity mechanism of tRNA precursor 5' in eyreum. On September 28,
, the important study was published online in a long text in science, an international authoritative academic journal.
tRNA as an important type of RNA molecule in the body, it is first of all the form of the previous body is transcribed, with immature 5' and 3' ends, where 5' end maturity needs to be the evolution very conservative RNA-protein complex RNase P to be catalyzed.
RNase P is present in all species on Earth and is essential for life activity, a nuclease mediated by RNA and responsible for the catalytic reaction of tRNA precursors. RNase P, a
eukala, is a molecular machine consisting of a long-chain, non-coding RNA molecule (-300nt) and nearly ten protein subunits.
However, little is known about the assembly form of RNase P in eukaryotic organisms and its substrate identification and catalytic mechanisms.
to this end, the Thunder team successfully parsed the structure of the yeast endogenous RNase P whole enzyme and its compound with the substrate pre-tRNA, which reveals the tissue form of the spatial atomic resolution of RNase P sub-sub-sub-cells in eukaryosenic organisms, where the protein sub-bases are closely intertwined to stabilize the structure of the RNA catalytic sub-sub-cells.
also found that RNase P identifies tRNA precursors with a "double anchor" mechanism. the 5' end of the
tRNA is specifically anchored at the catalytic center to induce it to complete the cutting reaction. the binding of
" substrate tRNA induces a huge conformational change in a key residue of the enzyme catalytic center.
" Thunder researchers told China Science Daily that, combined with molecular dynamics simulations, they proposed a double magnesium ion model of RNase P catalytic reaction, which further explains the catalytic molecular mechanism of this ancient nuclease.
experts in the field of nucleases believe that this landmark study has for the first time completely proposed the mature molecular mechanism of the eyrebiotic RNase P catalytic substrate tRNA precursor cutting, which is a major breakthrough in the field of nuclease and RNA structural biology.
antibiotic resistance has become a major threat to human health, RNase P and ribosomes, as the only two naturally present in all species of conservative nuclease, are important targets of antibiotic-type drugs.
therefore, RNase P as a potential target for new antibiotics, the structural study of this class of ancient nucleases will provide an important molecular basis for the subsequent design of new antibiotics.
it is understood that Lan Pengfei, assistant researcher of the Institute of Precision Medicine of the Ninth People's Hospital, Dr. Tam Ming of the Leiming Research Group, and Zhang Yuebin, associate researcher of dalian Chemical Institute of the Chinese Academy of Sciences, are the co-first authors of the paper;
the study was funded by the National Nature Fund project and the Chinese Academy of Sciences Strategic Pilot Project (Category B).
Source: Science.com.