Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Molecular Biology
Multicopy Suppression Of Ribosomal Protein Deletion Mutants, Jacqualine Cerbone
Multicopy Suppression Of Ribosomal Protein Deletion Mutants, Jacqualine Cerbone
Senior Honors Projects
To suppress the ribosome assembly defective phenotype of a ribosomal protein uS17- deficient mutant, various ribosomal proteins were used to act as multicopy suppressors. Ribosomal protein uS17 is a highly conserved component of the 30S (small) ribosomal subunit and is important for 30S subunit assembly. Mutants with a deletion of rpsQ (the gene encoding uS17) are viable but have a severe 30S subunit assembly defect and a temperature-sensitive (ts) phenotype. While fully assembled 30S subunits do form, incomplete ("20S") particles lacking several proteins accumulate. We hypothesized that increasing the intracellular concentration of one or more of the proteins missing from …
Establishing A Biochemical System For The Purification And Atpase Activity Of Gst-Dbp5, Sarah R. Utley, Rachel E. Rigsby Phd, Rebecca L. Adams Phd
Establishing A Biochemical System For The Purification And Atpase Activity Of Gst-Dbp5, Sarah R. Utley, Rachel E. Rigsby Phd, Rebecca L. Adams Phd
Science University Research Symposium (SURS)
The export of mRNA out of the nucleus is a crucial step for eukaryotic gene expression. The export of mRNA transcripts is aided by Mex67, which allows export through the nuclear pore complex doorways in the nuclear envelope. Once out of the nucleus, a protein known as Dbp5, bound to ATP, Gle1, and Nup42 aids in the directionality of mRNA export by helping remove Mex67 from the mRNA strand. Following interaction with RNA, Dbp5 then hydrolyzes ATP so that it unbinds the mRNA, allowing for enzyme recycling. Previous efforts worked towards the purification of Dbp5, but the attempts were unsuccessful …