Interaction of Human Ribosomal Protein S26 with Fragments of Its Own mRNA and Pre-mRNA in Nuclear Extract of HeLa Cells |
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Authors: | Ivanov A V Malygin A A Karpova G G |
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Institution: | (1) Novosibirsk Institute of Bioorganic Chemistry, Siberian Division, Russian Academy of Sciences, Novosibirsk, 630090, Russia |
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Abstract: | As shown by nitrocellulose filtration assays with RNA fragments transcribed from various regions of the human ribosomal protein (rp) S26 gene, recombinant rpS26 binds to the first intron of the rpS26 pre-mRNA (apparent association constant (K
a) 5.0 · 107 M–1) and, to a lesser extent, to the rpS26 mRNA (K
a 2.0 · 107 M–1). The binding was specific, since human rpS19 had an order of magnitude lower K
a with the first intron and did not bind with the rpS26 mRNA. Immunoassays with specific antibodies showed that rpS26 contained in the nuclear extract of HeLa cells binds to the first intron of its pre-mRNA and, less efficiently, to its mRNA. In either case, RNA binding substantially increased in the presence of recombinant rpS26. Along with other (48K, 59K) nuclear proteins, rpS26 was assumed to form complexes, the functional role of which is storage of pre-mRNAs inactive in splicing. |
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Keywords: | human ribosomal protein S26 mRNA pre-mRNA recombinant rpS26 antibodies to rpS26 interaction of ribosomal proteins with RNA nuclear extract of HeLa cells |
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