The canonical single-stranded DNA-binding protein is not an essential replication factor but an RNA chaperon in Saccharolobus islandicus.
The canonical single-stranded DNA-binding protein is not an essential replication factor but an RNA chaperon in Saccharolobus islandicus.
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DOI：
10.1016/j.isci.2023.108389
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发表时间：
2023-12-15
期刊：
影响因子：
5.8
通讯作者：
Shen, Yulong
中科院分区：
文献类型：
--
作者：
Xiao, Yuanxi;Jiang, Zhichao;Zhang, Mengqi;Zhang, Xuemei;Gan, Qi;Yang, Yunfeng;Wu, Pengju;Feng, Xu;Ni, Jinfeng;Dong, Xiuzhu;She, Qunxin;Huang, Qihong;Shen, Yulong
单链DNA结合蛋白（SSBs）被认为是不可缺少的复制因子。在此，我们报告的基因编码的典型SSB（SisSSB）和非典型SSB（SisDBP）在Eisolobus islandicus REY 15 A细胞活力不是必不可少的。有趣的是，在较低的温度（55°C）下，SisSSB的蛋白水平增加，ΔSisssb和ΔSisssbΔSisdbp的生长被延迟。SisSSB在体外对dsRNA和DNA/RNA杂合体具有解链活性，并且能够在大肠杆菌中解链RNA发夹。此外，核心SisSSB结构域能够补充大肠杆菌中冷休克蛋白的缺失。重要的是，这些活动是保守的典型SSB从Crenarchaeota物种，缺乏细菌Csp同源物。总的来说，我们的研究已经阐明了古细菌典型SSBs的功能，这些SSBs不作为DNA加工因子发挥作用，但在需要dsRNA或DNA/RNA杂交体解链的过程中发挥作用。两种已知的单链DNA结合蛋白在古菌中不是必需的SisSSB在体外表现出解链活性dsRNA在大肠杆菌中解旋RNA发夹SisSSB作为冷休克蛋白，促进温度降档适应dsRNA解链活性在缺乏Csp同系物的泉古菌中是保守的细菌学;生物科学;微生物学;分子生物学
Single-stranded DNA-binding proteins (SSBs) have been regarded as indispensable replication factors. Herein, we report that the genes encoding the canonical SSB (SisSSB) and the non-canonical SSB (SisDBP) in Saccharolobus islandicus REY15A are not essential for cell viability. Interestingly, at a lower temperature (55°C), the protein level of SisSSB increases and the growth of ΔSisssb and ΔSisssbΔSisdbp is retarded. SisSSB exhibits melting activity on dsRNA and DNA/RNA hybrid in vitro and is able to melt RNA hairpin in Escherichia coli. Furthermore, the core SisSSB domain is able to complement the absence of cold-shock proteins in E. coli. Importantly, these activities are conserved in the canonical SSBs from Crenarchaeota species that lack bacterial Csp homologs. Overall, our study has clarified the function of the archaeal canonical SSBs which do not function as a DNA-processing factor, but play a role in the processes requiring melting of dsRNA or DNA/RNA hybrid. Two known single-stranded DNA-binding proteins are not essential in and archaeon SisSSB exhibits melting activity dsRNA in vitro and unwinds RNA hairpin in E. coli SisSSB acts as a cold-shock protein, facilitating temperature downshift adaption The dsRNA melting activity is conserved in Crenarchaea that lack Csp homolog Bacteriology; Biological sciences; Microbiology; Molecular biology
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