Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E.
Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E.
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DOI：
10.1093/nar/gki505
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发表时间：
2005
影响因子：
14.9
通讯作者：
Putzer H
中科院分区：
文献类型：
--
作者：
Even S;Pellegrini O;Zig L;Labas V;Vinh J;Bréchemmier-Baey D;Putzer H
许多原核生物缺乏RNase E的等价物，其在大肠杆菌中的mRNA降解中起关键作用。本文报道了枯草芽孢杆菌中两种旁系同源核糖核酸内切酶的纯化和质谱鉴定，命名为RNase J1和J2，它们与RNase E具有功能同源性，但没有序列相似性。两种酶都能在大肠杆菌RNase E也能切割的位点切割枯草B.subtilis thrS前导序列。我们以前已经表明，在这个网站的切割增加了下游信使的稳定性。此外，RNase J1/J2以位点特异性方式对底物的5′磷酸化状态敏感。RNases J1/J2属于金属β-内酰胺酶家族，在许多原核生物中具有进化上的保守性，是一个新的内切核糖核酸酶家族。RNA酶J1/J2似乎与特定mRNA的调节加工/成熟有关，例如T-box家族成员thrS和thrZ，但也可能有助于整体mRNA降解。
Many prokaryotic organisms lack an equivalent of RNase E, which plays a key role in mRNA degradation in Escherichia coli. In this paper, we report the purification and identification by mass spectrometry in Bacillus subtilis of two paralogous endoribonucleases, here named RNases J1 and J2, which share functional homologies with RNase E but no sequence similarity. Both enzymes are able to cleave the B.subtilis thrS leader at a site that can also be cleaved by E.coli RNase E. We have previously shown that cleavage at this site increases the stability of the downstream messenger. Moreover, RNases J1/J2 are sensitive to the 5′ phosphorylation state of the substrate in a site-specific manner. Orthologues of RNases J1/J2, which belong to the metallo-β-lactamase family, are evolutionarily conserved in many prokaryotic organisms, representing a new family of endoribonucleases. RNases J1/J2 appear to be implicated in regulatory processing/maturation of specific mRNAs, such as the T-box family members thrS and thrZ, but may also contribute to global mRNA degradation.