The products of the A genes of bacteriophages Mu of Escherichia coli and D3112 of Pseudomonas aeruginosa are required for the transposition of the double-stranded DNA genomes of their respective phages. Mutant proteins of the multifunctional Mu transposase were constructed in vitro in order to locate regions of the enzyme that may be important for function. Deletions in the Mu A gene yielded two mutant proteins that help to define the end-specific DNA-binding domain. The insertion of two or four amino acids at eight different sites produced six mutant transposase proteins that were inhibited for $ mu$Mu transposition in vivo, but not DNA binding in vitro, at 37$ sp circ$C. In addition, site-specific mutagenesis was performed to alter tyrosine 414, an amino acid which is situated in a region that displays amino acid homology to the active sites of other nicking-closing enzymes. / The A and B genes of transposable phage D3112 were cloned and sequenced in order to compare their gene products to those from the analogous genes of ccliphage Mu. (Abstract shortened by UMI.)
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.28946 |
| Date | January 1994 |
| Creators | Ulycznyj, Peter I. |
| Contributors | DuBow, Michael S. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Doctor of Philosophy (Department of Microbiology and Immunology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001440687, proquestno: NN05806, Theses scanned by UMI/ProQuest. |
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