2026-10-07T13:16:50Z
https://api.figshare.com/v2/oai
oai:figshare.com:article/34047611
2026-10-01T17:26:03Z
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<p>Primers used in this study.</p>
Kateřina Abrhámová (4739808)
Alexandra Gredová (25157630)
Karolína Navrátilová (25157633)
Mohamed Boumaiza (5636147)
Petr Folk (209900)
Biophysics
Biochemistry
Microbiology
Genetics
Molecular Biology
Chemical Sciences not elsewhere classified
Biological Sciences not elsewhere classified
Developmental Biology
Cancer
Virology
intergenic regulation mediated
first catalytic step
5 ’ ss
div >< p
additional stem loops
tested splicing efficiency
saccharomyces cerevisiae </
rather stalled splicing
enhanced splicing inhibition
intron binding using
predicted stem
alternate stem
p structure
permitted splicing
b </
structural ensemble
rpl22 </
ribosomal roles
ribosomal proteins
regulatory mechanism
prevent recognition
predicted features
particular type
others described
mutagenesis identified
mrna behaves
later stage
hybrid system
fulfill non
containing reporter
branch point
binding capacity
allosteric switch
<div><p>Ribosomal proteins, because of their RNA-binding capacity, may engage various cellular RNAs and fulfill non-ribosomal roles. Previously, we and others described the intergenic regulation mediated by splicing of <i>RPL22</i> paralogs in <i>Saccharomyces cerevisiae</i>. Here, we prepared a panel of <i>RPL22A/B</i> intronic mutants with respect to their RNAfold-predicted features and analyzed their properties. We tested splicing efficiency and Rpl22-intron binding using an intron-containing reporter and a yeast three-hybrid system, respectively. We found that the splicing of <i>RPL22</i> introns can be inhibited by stabilizing a predicted stem as part of a particular type of conformation (I structure). Stabilizing the formation of an alternate stem (P structure) permitted splicing. Binding of the Rpl22 protein to the intron led to enhanced splicing inhibition in WT and several of the mutants, which we interpret as stabilization of the I structure. Mutagenesis identified both the main and alternative 5’ss and additional stem loops as part of the regulatory mechanism. The inhibitory conformation of the intron did not prevent recognition of the 5’ss and branch point, but rather stalled splicing at a later stage, before the first catalytic step. We conclude that the structural ensemble of the <i>RPL22</i> pre-mRNA behaves as an allosteric switch that responds to Rpl22 concentration.</p></div>
2026-10-01T17:25:45Z
Dataset
Dataset
10.1371/journal.pone.0359197.s014
https://figshare.com/articles/dataset/_p_Primers_used_in_this_study_p_/34047611
CC BY 4.0