Thesis (Ph. D.)--Virginia Polytechnic Institute and State University, 1990. / Vita. Abstract. Includes bibliographical references (leaves 114-115). Also available via the Internet.

Thesis (Ph. D.)--University of Idaho, 2005. / Also available online in PDF format. Abstract. "December 2005." Includes bibliographical references.

No description available.

Diverse research into the model organism, Escherichia coli, has added substantial depth to our understanding of genome editing of bacteria. Recombineering using the λ Red system is the most disruptive molecular technology discovered thus far, and improved our ability to introduce targeted single nucleotide variants by ~1E4 fold. This discovery has catalyzed incredible progress and enabled ambitious genome/organism engineering projects such as high throughput metabolic engineering to genome-wide codon reassignment. While efforts in E. coli have since accelerated further, work in other bacterial model organisms has lacked this catalyst and continues to fall behind E. coli. To facilitate development of disruptive technologies for non-standard model organisms, we produced a library of homologs to the λ Red recombinase, λ β (NP_040617.1), to generate a toolbox for recombinase discovery in organisms with minimal tools. We demonstrated the recombinase discovery workflow, called Serial Evolutionary Enrichment for Recombinases (SEER), in E. coli and present a number of alternatives to using λ Red for genome editing. We then moved on to explore λ β-mediated recombination in vitro where we able to show that bet specifically unloads E. coli Ssb from Ssb-coated oligos to facilitate annealing. We hypothesized that ssb represents the minimal host interaction node that a recombinase must achieve to facilitate recombination in vivo, and demonstrated a gain-of-function phenotype when species-matched recombinase/ssb pairs are ported into foreign organisms, potentially opening up poorly understood organisms to recombineering using well understood recombinase/ssb pairs.

No description available.

Expression of cDNA clones of the M1 double-stranded RNA killer preprotoxin coding region in Saccharomyces cerevisiae successfully directed the synthesis of secreted active toxin. Transformants harbouring these expression plasmids also displayed a K1 specific immunity phenotype. Immunoprecipitation of intracellular proteins with antitoxin antiserum showed that these transformants synthesize a 42kd glycosylated preprotoxin precursor. Two smaller unglycosylated immunoreactive species could also be resolved. These toxin precursor species were characterized by using secretory-defective hosts, by comparative electrophoretic mobilities, and by tunicamycin susceptibility. Such studies indicate that these protein species represent intermediates generated by signal cleavage of the preprotoxin and its subsequent glycosylation and provide evidence that these events occur post-translationally. Mutational analysis of the 44 amino acid preprotoxin N-terminal leader indicated that it is functionally bipartite, consisting of an N-terminal signal sequence and a C-terminal pro-sequence. Deletion of the leader perturbed but did not eliminate secretion of toxin.

No description available.

Thesis (M.S.)--Rochester Institute of Technology, 2009. / Typescript. Includes bibliographical references (leaves 56-59).

Thesis (Ph.D.)--University of California, San Francisco, 2004. / Includes bibliographical references. Also available online.

Thesis (Ph. D.)--Washington State University, May 2009. / Title from PDF title page (viewed on June 8, 2009). "School of Electrical Engineering and Computer Science." Includes bibliographical references.