Presentation Type

Presentation

Full Name of Faculty Mentor

Michelle Barthet, Biology

Major

Biology

Presentation Abstract

Structural and biochemical evidence links group II introns as evolutionary precursors of nuclear introns. The spliceosome binds and excises nuclear introns. Maturases are prokaryotic enzymes that aid group II intron excision. The evolutionary ties between group II introns and nuclear introns suggest a possible link between maturases and the nuclear spliceosome. Structural analysis of Prp8, a core enzyme of the nuclear spliceosome has demonstrated this link and revealed similarity to prokaryotic maturases. Maturase K (MatK) is a chloroplast group II intron maturase. Unlike prokaryotic maturases, MatK binds to multiple intron substrates suggesting possible evolution akin to the nuclear spliceosome machinery. In the chloroplasts, MatK is responsible for the splicing of 7 plastid-encoded introns. We investigated protein interactions of the MatK maturase using co-immunoprecipitation. We determined similarities to proteins that interact with nuclear Prp8 ribonucleoprotein complex. This data supports MatK as a model of early evolution of the nuclear spliceosome.

Location

Virtual Session Room 2

Start Date

22-4-2021 1:20 PM

End Date

22-4-2021 1:40 PM

Disciplines

Biology

Included in

Biology Commons

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Apr 22nd, 1:20 PM Apr 22nd, 1:40 PM

Homology of a Maturase to the Heart of the Nuclear Spliceosome

Virtual Session Room 2

Structural and biochemical evidence links group II introns as evolutionary precursors of nuclear introns. The spliceosome binds and excises nuclear introns. Maturases are prokaryotic enzymes that aid group II intron excision. The evolutionary ties between group II introns and nuclear introns suggest a possible link between maturases and the nuclear spliceosome. Structural analysis of Prp8, a core enzyme of the nuclear spliceosome has demonstrated this link and revealed similarity to prokaryotic maturases. Maturase K (MatK) is a chloroplast group II intron maturase. Unlike prokaryotic maturases, MatK binds to multiple intron substrates suggesting possible evolution akin to the nuclear spliceosome machinery. In the chloroplasts, MatK is responsible for the splicing of 7 plastid-encoded introns. We investigated protein interactions of the MatK maturase using co-immunoprecipitation. We determined similarities to proteins that interact with nuclear Prp8 ribonucleoprotein complex. This data supports MatK as a model of early evolution of the nuclear spliceosome.