The 3′UTR-derived sRNA RsaG coordinates redox homeostasis and metabolism adaptation in response to glucose-6-phosphate uptake in Staphylococcus aureus
The 3′UTR-derived sRNA RsaG coordinates redox homeostasis and metabolism adaptation in response to glucose-6-phosphate uptake in Staphylococcus aureus
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DOI：
10.1111/mmi.14845
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发表时间：
2021-11-25
影响因子：
3.6
通讯作者：
Caldelari, Isabelle
中科院分区：
文献类型：
--
作者：
Desgranges, Emma;Barrientos, Laura;Caldelari, Isabelle
金黄色葡萄球菌（Staphylococcus aureus）RsaG是来自保守的uhpT基因的3 '-非翻译区（3' UTR）衍生的sRNA，其编码响应于细胞外G6 P而表达的葡萄糖-6-磷酸（G6 P）转运蛋白。转录本uhpT-RsaG在核糖核酸外切酶J1/J2的作用下从5 '端降解到3'端，其被RsaG 5 '端的稳定发夹结构阻断，导致其积累。当细菌内化到宿主细胞中或在粘液分泌细胞存在下，RsaG与uhpT一起被诱导。使用MS 2亲和纯化结合RNA测序，鉴定了几种RNA作为靶标，包括编码转录因子雷克斯、CcpA、SarA和sRNA Rsal的mRNA。我们的数据表明，RsaG有助于控制氧化还原稳态和调节代谢，以改变环境条件。RsaG使用不同的分子机制来稳定、降解或抑制其mRNA靶标的翻译。虽然RsaG仅在近缘物种中保守，但猿病原体S.猿猴携带一种sRNA，其序列高度不同，并且不响应G6 P水平。我们的研究结果假设来自UhpT转运蛋白编码mRNA的3 'UTR可以快速进化以适应宿主生态位。
Staphylococcus aureus RsaG is a 3'-untranslated region (3'UTR) derived sRNA from the conserved uhpT gene encoding a glucose-6-phosphate (G6P) transporter expressed in response to extracellular G6P. The transcript uhpT-RsaG undergoes degradation from 5'- to 3'-end by the action of the exoribonucleases J1/J2, which are blocked by a stable hairpin structure at the 5'-end of RsaG, leading to its accumulation. RsaG together with uhpT is induced when bacteria are internalized into host cells or in the presence of mucus-secreting cells. Using MS2-affinity purification coupled with RNA sequencing, several RNAs were identified as targets including mRNAs encoding the transcriptional factors Rex, CcpA, SarA, and the sRNA Rsal. Our data suggested that RsaG contributes to the control of redox homeostasis and adjusts metabolism to changing environmental conditions. RsaG uses different molecular mechanisms to stabilize, degrade, or repress the translation of its mRNA targets. Although RsaG is conserved only in closely related species, the uhpT 3'UTR of the ape pathogen S. simiae harbors an sRNA, whose sequence is highly different, and which does not respond to G6P levels. Our results hypothesized that the 3'UTRs from UhpT transporter encoding mRNAs could have rapidly evolved to enable adaptation to host niches.