Nexus between RNA conformational dynamics and functional versatility DOI
Yun-Tzai Lee

Current Opinion in Structural Biology, Год журнала: 2024, Номер 89, С. 102942 - 102942

Опубликована: Окт. 15, 2024

Язык: Английский

Structural basis of 3′-tRNA maturation by the human mitochondrial RNase Z complex DOI Creative Commons
Genís Valentín Gesé, B.M. Hallberg

The EMBO Journal, Год журнала: 2024, Номер unknown

Опубликована: Ноя. 8, 2024

Язык: Английский

Процитировано

3

Engineering of RNase P Ribozymes for Therapy against Human Cytomegalovirus Infection DOI Creative Commons
Adam W. Smith, Isadora Zhang,

Phong Trang

и другие.

Viruses, Год журнала: 2024, Номер 16(8), С. 1196 - 1196

Опубликована: Июль 25, 2024

Nucleic acid-based gene interference and editing strategies, such as antisense oligonucleotides, ribozymes, RNA (RNAi), CRISPR/Cas9 coupled with guide RNAs, are exciting research tools show great promise for clinical applications in treating various illnesses. RNase P ribozymes have been engineered therapeutic against human viruses cytomegalovirus (HCMV). M1 ribozyme, the catalytic subunit of from

Язык: Английский

Процитировано

1

Divergent molecular assembly and catalytic mechanisms between bacterial and archaeal RNase P in pre-tRNA cleavage DOI Creative Commons
Xiaoge Liang, Dian Chen, Ai-Min Su

и другие.

Proceedings of the National Academy of Sciences, Год журнала: 2024, Номер 121(43)

Опубликована: Окт. 16, 2024

Ribonuclease P (RNase P) plays a vital role in the maturation of tRNA across bacteria, archaea, and eukaryotes. However, how RNase assembles various components to achieve specific cleavage precursor (pre-tRNA) different organisms remains elusive. In this study, we employed single-molecule fluorescence resonance energy transfer probe dynamics from E. coli ( Escherichia ) Mja Methanocaldococcus jannaschii during pre-tRNA by incorporating five Cy3-Cy5 pairs into P. Our results revealed significant differences assembly catalytic mechanisms between at both RNA protein levels. Specifically, Eco RPR) can adopt an active conformation that is capable binding cleaving with high specificity independently. The addition component (RnpA) enhances accelerates efficiency increasing stabilizing conformation. contrast, RPR unable form catalytically on its own, least four proteins are required induce correct folding RPR. Mutation experiments suggest functional deficiency arises absence second structural layer, proper intermolecular essential for be over broad temperature range. We propose models illustrate distinct patterns RNA–protein interactions these two organisms.

Язык: Английский

Процитировано

1

Nexus between RNA conformational dynamics and functional versatility DOI
Yun-Tzai Lee

Current Opinion in Structural Biology, Год журнала: 2024, Номер 89, С. 102942 - 102942

Опубликована: Окт. 15, 2024

Язык: Английский

Процитировано

0