Date of Award
Bachelor of Science (BS)
College of Science
Michelle M. Barthet
Maturase K (MatK) is the only group II intron encoded protein in the chloroplast of land plants. Maturases are prokaryotic enzymes that catalyze formation of the lariat structure needed for intron removal from precursor RNAs. The chloroplast maturase MatK, is a descendant of prokaryotic maturases, however, unlike its prokaryotic relatives, MatK is thought to catalyze excision of, not only its own intron, but also the introns of other group II introns in the plastome. Similar to the multiprotein and snRNA spliceosomal complex of the nucleus, it is postulated that MatK is not working alone to excise these introns but most likely requires additional protein factors to facilitate intron excision. In order to identify proteins that interact with MatK and understand more about splicing in the chloroplast, several laboratory methods were employed. Chloroplasts were extracted from the model organism O. sativa japonica and used in a co-Immunoprecipitation with anti-MatK antibody to obtain MatK and the proteins that bind to it. 2D gel electrophoresis was used to separate the proteins obtained, along with subsequent protein identification using electrospray ionization mass spectrometry.
Angello, Lauren, "Use of Co-Immunoprecipitations and 2D Gel Electrophoresis to Identify Protein-Protein Interactions of Maturase K" (2018). Honors Theses. 355.
Available for download on Sunday, January 17, 2021