无 RNA 和最小化的 RNase P 在... 中。
Minimal and RNA-free RNase P in .
机构信息
Institute of Pharmaceutical Chemistry, Philipps-Universität Marburg, 35037 Marburg, Germany.
Faculty of Chemistry, Mass Spectrometry, Philipps-Universität Marburg, 35032 Marburg, Germany.
出版信息
Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11121-11126. doi: 10.1073/pnas.1707862114. Epub 2017 Oct 3.
Abstract
RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium : Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of and strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that and related likely acquired HARP by horizontal gene transfer from an archaeon.
摘要
RNase P 是所有生命领域中必需的 tRNA 加工酶。我们在嗜热菌中发现了一种未知类型的仅由蛋白质组成的 RNase P。这种酶没有 RNA 亚基，是同类中最小的，由仅 23kDa 的多肽组成，仅包含金属核酸酶结构域。该蛋白在体外具有 RNase P 活性，并挽救了其更复杂和更大的内源性核糖核蛋白 RNase P 失活的 和 菌株的生长。在许多古菌和一些细菌中鉴定出了 RNase P（HARP）的同源物，其中所有古菌和大多数细菌也编码基于 RNA 的 RNase P；在两个选定的案例中，可以验证来自同一细菌或古菌的两种 RNase P 形式的活性。生物信息学分析表明， 和相关的 可能通过水平基因转移从古菌中获得了 HARP。
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