Title |
Structures of the Klebsiella oxytoca phage Phi KO2 and vibrio harveyi myovirus-like protelomerase far C-terminal domains |
Publication Type |
dissertation |
School or College |
College of Pharmacy |
Department |
Medicinal Chemistry |
Author |
Smith, Diana K. |
Date |
2010-08 |
Description |
A small but growing number of bacteria and phages are known to contain linear, hairpin-ended genomes. The hairpin "protelomeres" are created by the action of a dedicated enzyme known as protelomerase that acts on a palindromic DNA target sequence. Phage protelomerases are typically longer than their bacterial counterparts and contain an additional far C-terminal region of limited sequence conservation. Studies of the protelomerase of the Klebsiella oxytoca phage ΦKO2 have shown that although the far C-terminal region is not required to produce hairpin ends, truncation of the region has a drastic effect on enzyme kinetics. To date, no other studies have been reported on the far C-terminal region of this or any other protelomerase. We present the solution structures of the far C-terminal regions of two phage protelomerases. The regions form homologous, compact structures that adopt a fold similar to the canonical double-stranded RNA-binding domain and have been called the far C-terminal domains. Sequence alignment and secondary structure predictions show that all known and putative phage protelomerases contain C-terminal regions which will almost certainly form homologous domains. A sequence comparison of these proteins with all known protelomerases is presented, along with an analysis of the sequence and structure of proteins which adopt a similar fold. Based on structure homology and comparative sequence conservation of key binding regions, we propose that the domain belongs to the growing family of three stranded β-sheet DNA-binding proteins that is a subclass of the double-stranded RNA-binding domain superfamily. |
Type |
Text |
Publisher |
University of Utah |
Subject MESH |
Klebsiella oxytoca; Enzyme Precursors; Telomerase; DNA-Directed DNA Polymerase; DNA Replication; Gene Expression Regulation, Enzymologic; RNA-Binding Proteins; Protein Binding; Protein Folding; DNA Hairpins; Oligonucleotides; Bacteriophages; Promoter Regions, Genetic; DNA-Binding Proteins; Viral Proteins |
Dissertation Institution |
University of Utah |
Dissertation Name |
Doctor of Philosophy |
Language |
eng |
Relation is Version of |
Digital reproduction of Structures of the Klebsiella Oxytoca Phage Phi KO2 and Vibrio Harveyi Myovirus-Like Protelomerase Far C-Terminal Domains. Spencer S. Health Sciences Library. Print version available at J. Willard Marriott Library Special Collections. |
Rights Management |
Copyright © Diana K. Smith 2010 |
Format |
application/pdf |
Format Medium |
application/pdf |
Format Extent |
3,397,792 bytes |
Source |
Original in Marriott Library Special Collections, QR6.5 2010.S64 |
ARK |
ark:/87278/s60k5hss |
Setname |
ir_etd |
ID |
196406 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s60k5hss |