SNORA

Last update 08 May 2025

Basic Info

Synonyms

H/ACA box snoRNAs

Introduction-

100 Clinical Results associated with SNORA

100 Translational Medicine associated with SNORA

0 Patents (Medical) associated with SNORA

1,452

Literatures (Medical) associated with SNORA

01 Jun 2025·Plant Physiology and Biochemistry

Molecular mechanisms of CAX3 involved in salt tolerance in Arabidopsis

Article

Author: Kim, DongGwan ; Bahmani, Ramin ; Hwang, Seongbin ; Modareszadeh, Mahsa

CAX3 is a vacuolar proton/cation exchanger. To examine the role of CAX3 in salt stress, transgenic Arabidopsis over-expressing AtCAX3 or NtCAX3 was challenged with NaCl. CAX3-expressing Arabidopsis (CAX3-Arabidopsis) exhibited higher salt tolerance, lower accumulation of Na⁺, and increased Ca²⁺ level compared with the control plants. In support of this, CAX3-Arabidopsis exhibited less uptake and a higher export rate of Na⁺, as well as greater uptake and reduced export rate of Ca²⁺. Regarding the lower Na ⁺ level, the expression of HKT1 (Na⁺ uptake from the xylem) was reduced, whereas that of SOS1 (Na⁺ exporter) was enhanced. Furthermore, the expression of CNGC10 (Ca²⁺ importer) was higher, whereas that of ACA8 and ACA10 (Ca²⁺ exporters) was lower in CAX3-Arabidopsis compared with control plants. Transgenic Arabidopsis exhibited less oxidative stress (superoxide, hydrogen peroxide, and malondialdehyde) but greater activity of antioxidant enzymes (catalase, glutathione reductase, and superoxide dismutase), in accordance with higher salt tolerance. Additionally, atcax3 knockout Arabidopsis exhibited opposite phenotypes compared with CAX3-expressing plants, including lower salt tolerance with increased Na⁺ level, lower Ca²⁺ content, and reduced SOS1 expression. CAX3-Arabidopsis exhibited higher abscisic acid level and stomatal closure. Together, these findings indicate that CAX3 enhances salt tolerance by reducing Na⁺ accumulation, reactive oxygen species, and stomatal opening by increasing Ca²⁺ levels in Arabidopsis.

20 Mar 2025·Nucleic Acids Research

Small nucleolar RNAs promote the restoration of muscle differentiation defects in cells from myotonic dystrophy type 1

Article

Author: Furling, Denis ; Mouly, Vincent ; Hubé, Florent ; Francastel, Claire ; Tellier, Gilles ; Boyarchuk, Ekaterina ; Bonnet, Hélène ; Bogard, Baptiste

AbstractRecently, the repertoire of human small nucleolar noncoding RNAs (snoRNAs) and their potential functions has expanded with the discovery of new snoRNAs and messenger RNA (mRNA) targets, for which snoRNA-guided modifications may influence their stability, translatability, and splicing. We previously identified snoRNAs that are abundant in healthy human muscle progenitor cells. In this study, we demonstrated that SNORA40 and SNORA70 loss-of-function impairs myogenic differentiation. Interestingly, gain-of-function can rescue impaired differentiation muscle progenitor cells in myotonic dystrophy type 1 (DM1). We identified cyclin D3 (CCND3) mRNA, which is partially located in the nucleolus, as a target for SNORA40 and SNORA70, which are required for its pseudouridylated status. Expression of the CCND3 protein is required for muscle progenitors to exit the cell-cycle when they are induced to differentiate. We revealed that this switch requires SNORA40/70. Finally, we observed that DM1 cells show reduced levels of SNORA40/70 and undetectable CCND3 protein. However, restoring normal levels of SNORA40/70 partially restored CCND3 protein expression, coinciding with improved cell fusion capacity in DM1 muscle progenitors. Collectively, these data suggest that this effect may stem from SNORA40/70-dependent pseudouridylation of CCND3 mRNA, emphasizing snoRNAs as key players in normal and pathological muscle differentiation.

04 Mar 2025·Proceedings of the National Academy of Sciences

A degenerate telomerase RNA directs telomeric DNA synthesis in lepidopteran insects

Article

Author: Podlevsky, Joshua D. ; Chen, Julian J.-L. ; L. Dunn, Phoebe ; Chow, Chi-Nga ; Chou, Yu-Shu ; Akhter, Khadiza ; Logeswaran, Dhenugen ; Liu, Tianxiang

Telomerase elongates telomeres to maintain chromosome stability in most eukaryotes. Despite extensive studies across eukaryotic kingdoms, the telomerase holoenzyme in arthropods remains poorly understood. In this study, we purify the telomerase ribonucleoprotein complex from the lepidopteran insect Spodoptera frugiperda (fall armyworm) and identify a copurified 135-nucleotide telomerase RNA (TR) component. This miniature S. frugiperda TR (sfTR), the smallest TR known to date, retains a universal pseudoknot structure and a structurally defined template. Despite its small size, sfTR assembles with the recombinant S. frugiperda telomerase reverse transcriptase (sfTERT) protein in vivo to reconstitute telomerase activity for the synthesis of insect telomeric DNA repeats (TTAGG)n. The sfTR gene, like other animal TR genes, features an snRNA-type RNA polymerase II promoter. Uniquely, the sfTR transcript harbors a 5′-7-methylguanosine (M 7 G) cap, as opposed to the more typical snRNA-type 2,2,7-trimethylguanosine (TMG) cap. The difference in 5′-cap is likely because sfTR lacks the H/ACA snoRNA biogenesis domain necessary for cap hypermethylation. Moreover, sfTR also lacks the CR4/5 regulatory domain that is indispensable in vertebrate TRs for telomerase activity. This degenerate sfTR complements an enigmatic sfTERT that is missing certain telomerase-specific elements yet catalytically active in the absence of sfTR. Thus, insects have evolved a simplified telomerase, consisting of a small noncoding RNA that retains only minimal attributes essential for telomerase function. The simplified insect telomerase demonstrates a plausible evolutionary pathway for the emergence of telomerase ribonucleoprotein complex, arising from an ancient reverse transcriptase associated with a simple templating RNA component in early eukaryotes.

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