同源重组
计算生物学
核酸内切酶
细胞生物学
生物
功能(生物学)
DNA
遗传学
化学
作者
Hao Wu,Yubin Zheng,Adrian R. Laciak,Niu Huang,Mary Koszelak‐Rosenblum,Andrew Flint,Grant Carr,Guangyu Zhu
标识
DOI:10.1007/5584_2022_724
摘要
Three human nucleases, SNM1A, SNM1B/Apollo, and SNM1C/Artemis, belong to the SNM1 gene family. These nucleases are involved in various cellular functions, including homologous recombination, nonhomologous end-joining, cell cycle regulation, and telomere maintenance. These three proteins share a similar catalytic domain, which is characterized as a fused metallo-β-lactamase and a CPSF-Artemis-SNM1-PSO2 domain. SNM1A and SNM1B/Apollo are exonucleases, whereas SNM1C/Artemis is an endonuclease. This review contains a summary of recent research on SNM1's cellular and biochemical functions, as well as structural biology studies. In addition, protein structure prediction by the artificial intelligence program AlphaFold provides a different view of the proteins' non-catalytic domain features, which may be used in combination with current results from X-ray crystallography and cryo-EM to understand their mechanism more clearly.
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