The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H.
The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H.
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DOI:
10.3389/fmicb.2022.1034811
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发表时间:
2022
影响因子:
5.2
通讯作者:
Lu, Zheng
中科院分区:
文献类型:
--
作者:
Pang, Jing;Guo, Qinyu;Lu, Zheng
Ribonucleoside monophosphates are inevitably misincorporated into the DNA genome inside cells, and they need to be excised to avoid chromosome instability. Ribonucleases H (RNases H) are enzymes that specifically hydrolyze the RNA strand of RNA/DNA hybrids or the RNA moiety from DNA containing a stretch of RNA, they therefore are required for DNA integrity. Extensive studies have drawn a mostly clear picture of the mechanisms of RNase H catalysis, but some questions are still lacking definitive answers. This review summarizes three alternative models of RNase H catalysis. The two-metal model is prevalent, but a three-metal model suggests the involvement of a third cation in catalysis. Apparently, the mechanisms underlying metal-dependent hydrolyzation are more complicated than initially thought. We also discuss the metal choices of RNases H and analyze how chemically similar cations function differently. Substrate and cleavage-site specificities vary among RNases H, and this is explicated in detail. An intriguing phenomenon is that organisms have diverse RNase H combinations, which may provide important hints to how rnh genes were transferred during evolution. Whether RNase H is essential for cellular growth, a key question in the study of in vivo functions, is also discussed. This article may aid in understanding the mechanisms underlying RNase H and in developing potentially promising applications of it.
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通讯作者:
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DOI:
10.1016/j.jbc.2021.100462
发表时间:
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期刊:
The Journal of biological chemistry
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DOI:
10.1006/bbrc.2001.5523
发表时间:
2001-09-07
影响因子:
3.1
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通讯作者:
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