The L30e ribosomal protein from S. cerevisiae binds to its transcript RNA more strongly than to its primary target helix 58 of ribosomal RNA

<p>In <em>S. cerevisiae</em>, ribosomal protein L30e, in addition to being an integral part of the ribosome, autoregulates its levels of expression by: 1) binding to its transcript, inhibiting splicing; and 2) to its messenger RNA, inhibiting translation. This work explores ribosomal protein L30e binding to two short RNA fragments that mimic RNA-L30e binding sites. The L30e has a 100-fold higher affinity for its own transcript mRNA than for the helix 58 ribosomal rRNA target. Site-directed mutagenesis studies suggest that L30e maintains the same interaction network in both RNAs. Thermodynamics of L30e binding to RNAs give a direct insight into the energetic and entropic characteristics of complexes in aqueous solution and nicely complement the structural views derived from existing X-ray crystallography and multidimensional NMR studies. Experimental data support the scenario that in yeast L30e binds to an already pre-formed RNA helix 58.</p>

Name thesis:degree_name

Doctor of Philosophy (PhD)

Level thesis:degree_level

Bryn Mawr only

Discipline thesis:degree_discipline

Chemistry

Year

2018

Author dc:creator

• Kokona, Bashkim

• Chemistry

Repository record dc:identifier

https://repository.brynmawr.edu/dissertations/185

OAI identifier oai:identifier

oai:repository.brynmawr.edu:dissertations-1187