1H, 13C and 15N assignment of stem-loop SL1 from the 5'-UTR of SARS-CoV-2

IF 0.8 4区生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2021-08-28 DOI:10.1007/s12104-021-10047-2

Christian Richter, Katharina F. Hohmann, Sabrina Toews, Daniel Mathieu, Nadide Altincekic, Jasleen Kaur Bains, Oliver Binas, Betül Ceylan, Elke Duchardt-Ferner, Jan Ferner, Boris Fürtig, J. Tassilo Grün, Martin Hengesbach, Daniel Hymon, Hendrik R. A. Jonker, Bozana Knezic, Sophie M. Korn, Tom Landgraf, Frank Löhr, Stephen A. Peter, Dennis J. Pyper, Nusrat S. Qureshi, Andreas Schlundt, Robbin Schnieders, Elke Stirnal, Alexey Sudakov, Jennifer Vögele, Julia E. Weigand, Julia Wirmer-Bartoschek, Kerstin Witt, Jens Wöhnert, Harald Schwalbe, Anna Wacker

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引用次数: 4

Abstract

The stem-loop (SL1) is the 5'-terminal structural element within the single-stranded SARS-CoV-2 RNA genome. It is formed by nucleotides 7–33 and consists of two short helical segments interrupted by an asymmetric internal loop. This architecture is conserved among Betacoronaviruses. SL1 is present in genomic SARS-CoV-2 RNA as well as in all subgenomic mRNA species produced by the virus during replication, thus representing a ubiquitous cis-regulatory RNA with potential functions at all stages of the viral life cycle. We present here the ¹H, ¹³C and ¹⁵N chemical shift assignment of the 29 nucleotides-RNA construct 5_SL1, which denotes the native 27mer SL1 stabilized by an additional terminal G-C base-pair.

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从SARS-CoV-2的5'-UTR中对茎环SL1的1H, 13C和15N进行定位

茎环(SL1)是单链SARS-CoV-2 RNA基因组中的5'端结构元件。它由核苷酸7-33组成，由不对称的内部环打断的两个短螺旋段组成。这种结构在冠状病毒中是保守的。SL1存在于基因组SARS-CoV-2 RNA以及病毒在复制过程中产生的所有亚基因组mRNA物种中，因此是一种普遍存在的顺式调控RNA，在病毒生命周期的所有阶段都具有潜在的功能。我们在这里提出了29个核苷酸- rna结构5_SL1的1H, 13C和15N化学位移分配，这表明由额外的末端G-C碱基对稳定的天然27mer SL1。

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来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.