气候变化领域集成服务门户(CCPortal): Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex

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DOI	10.1073/pnas.2020393118
	Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex
	Yang Y.; Harris K.A.; Widner D.L.; Breaker R.R.
发表日期	2021
ISSN	00278424
卷号	118 期号:9
英文摘要	The OLE (ornate, large, and extremophilic) RNA class is one of the most complex and well-conserved bacterial noncoding RNAs known to exist. This RNA is known to be important for bacterial responses to stress caused by short-chain alcohols, cold, and elevated Mg2+ concentrations. These biological functions have been shown to require the formation of a ribonucleoprotein (RNP) complex including at least two protein partners: OLE-associated protein A (OapA) and OLE-associated protein B (OapB). OapB directly binds OLE RNA with high-affinity and specificity and is believed to assist in assembling the functional OLE RNP complex. To provide the atomic details of OapB-OLE RNA interaction and to potentially reveal previously uncharacterized protein-RNA interfaces, we determined the structure of OapB from Bacillus halodurans alone and in complex with an OLE RNA fragment at resolutions of 1.0 Å and 2.0 Å, respectively. The structure of OapB exhibits a K-shaped overall architecture wherein its conserved KOW motif and additional unique structural elements of OapB form a bipartite RNA-binding surface that docks to the P13 hairpin and P12.2 helix of OLE RNA. These high-resolution structures elucidate the molecular contacts used by OapB to form a stable RNP complex and explain the high conservation of sequences and structural features at the OapB-OLE RNA-binding interface. These findings provide insight into the role of OapB in the assembly and biological function of OLE RNP complex and can guide the exploration of additional possible OLE RNA-binding interactions present in OapB. © This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
英文关键词	Alcohol toxicity; GNRA tetraloop; KOW motif; Mg2+ tolerance; Noncoding RNA
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180451
作者单位	Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8103, United States; Howard Hughes Medical Institute, YaleUniversity, New Haven, CT 06520-8103, United States; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103, United States
推荐引用方式 GB/T 7714	Yang Y.,Harris K.A.,Widner D.L.,et al. Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex[J],2021,118(9).
APA	Yang Y.,Harris K.A.,Widner D.L.,&Breaker R.R..(2021).Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex.Proceedings of the National Academy of Sciences of the United States of America,118(9).
MLA	Yang Y.,et al."Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex".Proceedings of the National Academy of Sciences of the United States of America 118.9(2021).