Specific Bacteriophage Coat Protein-Rna Interactions

The coat proteins of the group I bacteriophages translationally repress their replicase genes by binding specifically to a region around the initiation codon called the translational operator. A large number of operator variants have been synthesized by using RNA ligase and transcription of synthetic DNA by T7 RNA polymerase in order to examine the roles of the helical region and the bulged A residue in the specific RNA-R17 coat protein interaction. The affinity between coat protein and each variant was determined by a nitrocellulose filter binding assay. The data of the variants with base pair changes indicated that a stable hairpin loop secondary structure of the operator must be maintained, but any base pairs can be used. 14 different nucleotides were introduced to the bulged A position of these coat protein binding fragments. The data indicated that while functional groups on N$\sp1$, C$\sp2$, C$\sp6$, N$\sp7$ and 2$\sp\prime$OH of the bulged A can be substituted without greatly changing protein binding, bulky substituents cannot be tolerated at these positions.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

1988

Author dc:creator

• Wu, Huey-Nan

Contributors dc:contributor

• Uhlenbeck, Olke C.,

• Chemistry, Biochemistry

Identifier

(UMI)AAI8815441

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70568