Please use this identifier to cite or link to this item:
http://hdl.handle.net/11375/22700
Title: | Studies on the Mechanism of Prokaryotic Translational Termination |
Other Titles: | Prokaryotic Translational Termination |
Authors: | Buckingham-Hader, Karen |
Advisor: | Ganoza, M. C. Neilson, T. |
Department: | Biochemistry |
Keywords: | prokaryots;translation;termination |
Publication Date: | Dec-1983 |
Abstract: | Using an in vitro prokaryotic termination assay, it was demonstrated that sequences neighbouring UA are recognized by RF-1 and stimulate cleavage of ribosome-bound f-met-tRNA_fmet. The ability of UA to signal release depends upon the nature of nucleotides adjacent both 3' and 5' to this sequence. RF-1 exhibits different specificity when potential termination sequences are covalently linked to AUG within the same polynucleotide, as in mRNA. Under these circumstances, within certain base context, (1) UA functions as a termination signal, (2) UA-containing terminator signals can be read out of the AUG-aligned reading frame and (3) RF-1 competes with aminoacyl-tRNA for sequence UUA. Another factor has been discovered, which partially corrects the specificity of RF-1. This factor (designated Specificity Factor) appears to be a protein, or a protein-containing component, and enhances RF-1-mediated termination caused by UAA but inhibits termination caused by UA. The factors known to participate in protein synthesis are not responsible for conferring specificity to the RF-1-mediated termination reaction. For this reason, it is believed that the Specificity Factor may be a new protein. |
URI: | http://hdl.handle.net/11375/22700 |
Appears in Collections: | Digitized Open Access Dissertations and Theses |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
buckingham-hader_karen_1983Dec_masters.pdf | 4.87 MB | Adobe PDF | View/Open |
Items in MacSphere are protected by copyright, with all rights reserved, unless otherwise indicated.