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1.
Nucleic Acids Res ; 50(14): 8143-8153, 2022 08 12.
Artículo en Inglés | MEDLINE | ID: mdl-35801908

RESUMEN

Tandem repeats of guanine-rich sequences in RNA often form thermodynamically stable four-stranded RNA structures. Such RNA G-quadruplexes have long been considered to be linked to essential biological processes, yet their physiological significance in cells remains unclear. Here, we report a approach that permits the detection of RNA G-quadruplex structures that modulate protein translation in mammalian cells. The approach combines antibody arrays and RGB-1, a small molecule that selectively stabilizes RNA G-quadruplex structures. Analysis of the protein and mRNA products of 84 cancer-related human genes identified Nectin-4 and CapG as G-quadruplex-controlled genes whose mRNAs harbor non-canonical G-quadruplex structures on their 5'UTR region. Further investigations revealed that the RNA G-quadruplex of CapG exhibits a structural polymorphism, suggesting a possible mechanism that ensures the translation repression in a KCl concentration range of 25-100 mM. The approach described in the present study sets the stage for further discoveries of RNA G-quadruplexes.


Asunto(s)
G-Cuádruplex , Regiones no Traducidas 5' , Animales , Guanina/química , Humanos , Mamíferos/genética , Biosíntesis de Proteínas , ARN Mensajero/metabolismo
2.
Nucleic Acids Res ; 49(22): e132, 2021 12 16.
Artículo en Inglés | MEDLINE | ID: mdl-34581825

RESUMEN

Imaging the dynamics of proteins in living cells is a powerful means for understanding cellular functions at a deeper level. Here, we report a versatile method for spatiotemporal imaging of specific endogenous proteins in living mammalian cells. The method employs a bifunctional aptamer capable of selective protein recognition and fluorescent probe-binding, which is induced only when the aptamer specifically binds to its target protein. An aptamer for ß-actin protein preferentially recognizes its monomer forms over filamentous forms, resulting in selective G-actin staining in both fixed and living cells. Through actin-drug treatment, the method permitted direct monitoring of the intracellular concentration change of endogenous G-actin. This protein-labeling method, which is highly selective and non-covalent, provides rich insights into the study of spatiotemporal protein dynamics in living cells.


Asunto(s)
Aptámeros de Nucleótidos , Imagen Óptica/métodos , Proteínas/análisis , Actinas/análisis , Aptámeros de Nucleótidos/química , Colorantes Fluorescentes , Células HeLa , Humanos , Imagen Molecular/métodos , ARN/química , Imagen de Lapso de Tiempo
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