The making and breaking of tRNAs by ribonucleases

被引：0

作者：

Elder, Jessica J. H. ^{[1
]}

Papadopoulos, Ry ^{[2
,3
]}

Hayne, Cassandra K. ^{[2
]}

Stanley, Robin E. ^{[1
]}

机构：

[1] Natl Inst Environm Hlth Sci, Signal Transduct Lab, NIH, Res Triangle Pk, NC 27709 USA

[2] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA

[3] Univ Chicago, Dept Chem, Chicago, IL 60637 USA

来源：

TRENDS IN GENETICS | 2024年 / 40卷 / 06期

基金：

美国国家卫生研究院;

关键词：

CRYO-EM STRUCTURE; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; PROTEIN-SYNTHESIS; HUMAN ANGIOGENIN; XRN2; BINDING; EXOSOME; DEGRADATION; DECAY; SURVEILLANCE;

D O I：

10.1016/j.tig.2024.03.007

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Ribonucleases (RNases) play important roles in supporting canonical and noncanonical roles of tRNAs by catalyzing the cleavage of the tRNA phosphodiester backbone. Here, we highlight how recent advances in cryo-electron microscopy (cryo-EM), protein structure prediction, reconstitution experiments, tRNA sequencing, and other studies have revealed new insight into the nucleases that process tRNA. This represents a very diverse group of nucleases that utilize distinct mechanisms to recognize and cleave tRNA during different stages of a tRNA's life cycle including biogenesis, fragmentation, surveillance, and decay. In this review, we provide a synthesis of the structure, mechanism, regulation, and modes of tRNA recognition by tRNA nucleases, along with open questions for future investigation.

引用

页码：511 / 525

页数：15

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