Abstract
AtGRP2 (Arabidopsis thaliana glycine-rich protein 2) is a 19-kDa RNA-binding glycine-rich protein that regulates key processes in A. thaliana. AtGRP2 is a nucleo-cytoplasmic protein with preferential expression in developing tissues, such as meristems, carpels, anthers, and embryos. AtGRP2 knockdown leads to an early flowering phenotype. In addition, AtGRP2-silenced plants exhibit a reduced number of stamens and abnormal development of embryos and seeds, suggesting its involvement in plant development. AtGRP2 expression is highly induced by cold and abiotic stresses, such as high salinity. Moreover, AtGRP2 promotes double-stranded DNA/RNA denaturation, indicating its role as an RNA chaperone during cold acclimation. AtGRP2 is composed of an N-terminal cold shock domain (CSD) followed by a C-terminal flexible region containing two CCHC-type zinc fingers interspersed with glycine-rich sequences. Despite its functional relevance in flowering time regulation and cold adaptation, the molecular mechanisms employed by AtGRP2 are largely unknown. To date, there is no structural information regarding AtGRP2 in the literature. Here, we report the 1H, 15N, and 13C backbone and side chain resonance assignments, as well as the chemical shift-derived secondary structure propensities, of the N-terminal cold shock domain of AtGRP2, encompassing residues 1–90. These data provide a framework for AtGRP2-CSD three-dimensional structure, dynamics, and RNA binding specificity investigation, which will shed light on its mechanism of action.
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Data Availability
The 1H, 15N, and 13C chemical shift assignments generated and analyzed in this study are available at the Biological Magnetic Resonance Bank (BMRB) under entry 51870.
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Acknowledgements
We are thankful to the National Center for Nuclear Magnetic Resonance Jiri Jonas (CNRMN) at the National Center for Structural Biology and Bioimaging (CENABIO), Federal University of Rio de Janeiro, for access to instrumentation and excellent technical support. This article is dedicated to the memory of Marcia O. Dias.
Funding
This work was funded by grants from Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ), E-26/010.001923/2019 and E-26/200.977/2022, and by a grant from Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), 306710/2021-8, to A.S.P. K.C.P. received a graduate fellowship from Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) and FAPERJ.
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K.C.P. prepared the sample, collected the spectra, processed and analyzed the data, and wrote the first draft of the manuscript. G.S.M. participated in the experimental design and manuscript revision. F.C.L.A. participated in the experimental design and manuscript revision. A.S.P. participated in experimental design, manuscript revision, and funding.
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Pougy, K.C., Sachetto-Martins, G., Almeida, F.C.L. et al. 1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2. Biomol NMR Assign 17, 143–149 (2023). https://doi.org/10.1007/s12104-023-10133-7
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DOI: https://doi.org/10.1007/s12104-023-10133-7