Human ribosomal protein S16 inhibits excision of the first intron from its own pre-mRNA |
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Authors: | A V Ivanov N M Parakhnevitch A A Malygin G G Karpova |
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Institution: | 1.Institute of Chemical Biology and Fundamental Medicine, Siberian Branch,Russian Academy of Sciences,Novosibirsk,Russia |
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Abstract: | Recombinant human ribosomal protein S16 (rpS16) is shown to bind specifically to a fragment of its own pre-mRNA that includes
exons 1 and 2, intron 1, and part of intron 2, and to inhibit the splicing of the fragment in vitro. The weaker binding of
other recombinant human ribosomal proteins, S10 and S13, to this pre-mRNA fragment indicated that the binding of rpS16 was
specific. Besides, the poly(AU) and rpS16 mRNA fragment insignificantly affected the binding of rpS16 to its pre-mRNA, providing
another evidence that the interaction was specific. rpS16 specifically inhibited the splicing of the pre-mRNA fragment, whereas
recombinant rpS10 and rpS13 did not affect intron excision from this pre-mRNA fragment in contrast to rpS16. Those positions
in rpS16 pre-mRNA fragment that were protected by rpS16 from cleavage by RNases T1, T2, and V1 were found to be located closely
to the branch point and 3’ splice site in the pre-mRNA. The obtained results suggest the possibility of the autoregulation
of rpS13 pre-mRNA splicing through the feedback mechanism. |
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