University of Illinois at Urbana-Champaign
Biochemical and Genetic Analyses of Rna-Protein Interactions
Abstract
dc:descriptionThe coat protein from bacteriophage R17/MS2 functions to repress translation of replicase and functions to encapsidate the RNA genome of the phage. The coat protein accomplishes these functions by interacting with a 21 nucleotide stem-loop structure located within the translation initiation region of the bacteriophage replicase gene. A great deal is known about the genetics and biochemistry of the RNA-protein interaction; however, the mechanism of translational repression is unclear. One model has the coat protein sequestering the SD sequence and AUG start codon in secondary structure while another model suggests that coat protein blocks 16S rRNA access to the RNA by steric masking. A new method for the construction of RNA challenge phages in a single recombination reaction was employed to create several replicase translational operator variants which have the hairpin structure recognized by coat at varying distances from the ant gene of bacteriophage P22 to demonstrate the mechanism of repression to be masking. Applying this knowledge, RNA-protein interactions of other systems can be studied using the RNA challenge phage system.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Microbiology
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Fouts, Derrick Eugene
- Contributors dc:contributor
-
- Daniel W. Celander
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9812588
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/86721