NDLI: Human ribosomal protein S16 inhibits excision of the first intron from its own pre-mRNA

Content Provider	Springer Nature Link
Author	Ivav, A. V. Parakhnevitch, N. M. Malygin, A. A. Karpova, G. G.
Copyright Year	2010
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.
Starting Page	82
Ending Page	88
Page Count	7
File Format	PDF
ISSN	00268933
Journal	Molecular Biology
Volume Number	44
Issue Number	1
e-ISSN	16083245
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2010-03-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	pre-mRNA of human ribosomal protein S16 enzymatic footprinting regulation of splicing human ribosomal proteins RNA-protein interactions Human Genetics Biochemistry Life Sciences
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biophysics

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