In S. cerevisiae, 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.
","abstract_html":"<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>","abstract_has_math":false,"creators":["Kokona, Bashkim"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Bryn Mawr only","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-01-01T08:00:00Z","date_published":"2018-01-01T08:00:00Z","updated_at":"2026-07-24T01:23:46Z","subjects":["Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://repository.brynmawr.edu/dissertations/185","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Kokona, Bashkim"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Bryn Mawr only"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://repository.brynmawr.edu/dissertations/185"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["In S. cerevisiae, 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.
"]},{"key":"dc:title","label":"Title","values":["The L30e ribosomal protein from S. cerevisiae binds to its transcript RNA more strongly than to its primary target helix 58 of ribosomal RNA"]}]}],"canonical_facts":{"dc:creator":["Kokona, Bashkim"],"dc:description.abstract":["In S. cerevisiae, 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.
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