Proteins of the Ner/Nlp family have been characterized in order to identify the evolutionarily conserved protein domains important to their structure and function. The homologous DNA-bonding Ner proteins of closely related temperate coliphages Mu and D108 regulate the transcription and transposition of the phage genomes by binding to nonhomologous DNA operators. In order to precisely define the DNA-binding domains of Mu and D108 Ner, recombinant Mu and D108 ner genes were constructed and the DNA-binding and pseudoimmunity properties of the recombinant proteins were examined. / D3112 is a Mu-like transposable bacteriophage of Pseudomonas aeruginosa which was proposed to encode a ner-like gene termed cip. In order to determine if cip is equivalent to ner, the D3112 left end was sequenced. Six possible open reading frames (ORFs) for Cip were identified, yet none were found to be biochemically homologous to Ner. However, an E. coli gene (nlp) which encodes a Ner-like protein (Nlp) has recently been identified. This gene product, when overexpressed in a cya crp*l strain, stimulates expression of the mal operon. We have demonstrated that nlp is not essential for E. coli viability and stability. The nlp gene is transcribed in E. coli and sequences homologous to nlp have been identified in the Enterobacteriaceae, but not in Pseudomonas aeruginosa. These studies indicate that Nlp, like its Ner counterparts, may play an important regulatory role and that these functions may be mediated by conserved protein structures.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.70307 |
| Date | January 1992 |
| Creators | Autexier, Chantal |
| 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: 001302297, proquestno: AAINN74740, Theses scanned by UMI/ProQuest. |
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