Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes

被引:10
作者
Bhatta, Arjun [1 ,2 ]
Hillen, Hauke S. [1 ,2 ,3 ]
机构
[1] Univ Med Ctr Goettingen, Dept Cellular Biochem, Humboldtallee 23, D-37073 Gottingen, Germany
[2] Max Planck Inst Multidisciplinary Sci, Res Grp Struct & Funct Mol Machines, Fassberg 11, D-37077 Gottingen, Germany
[3] Univ Goettingen, Cluster Excellence Multiscale Bioimaging Mol Machi, D-37075 Gottingen, Germany
关键词
PRECURSOR-TRANSFER-RNA; SUBSTRATE RECOGNITION; CATALYTIC STRATEGIES; CLEAVAGE; COMPLEX; SUBUNIT; SITE; PURIFICATION; HYDROLYSIS; MATURATION;
D O I
10.1016/j.tibs.2022.05.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ribonuclease P (RNase P) enzymes are responsible for the 5 ' processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase Ps (PRORPs) can be found in all three domains of life and can be divided into two structurally different types: eukaryotic and pro-karyotic. Recent structural studies on members of both families reveal a surpris-ing diversity of molecular architectures, but also highlight conceptual and mechanistic similarities. Here, we provide a comparison between the different types of PRORP enzymes and review how the combination of structural, bio-chemical, and biophysical studies has led to a molecular picture of protein -mediated tRNA processing.
引用
收藏
页码:965 / 977
页数:13
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