Genetic and mechanistic studies of the bacteriophage lambda integrase protein

"Site-specific recombination between bacteriophage $\lambda$ and E. coli chromosomes starts with the formation of higher-order nucleoprotein complexes, called ""intasomes"", followed by a series of steps catalyzed by the phage-encoded integrase (Int). In order to study the functions of Int during recombination, Int mutants defective in in vivo excision were isolated and screened for proficiency in binding to the arm-type sites using challenge phage assays. Fifty-eight such mutants were obtained and were further characterized (1) for their ability to bind the P$\sp\prime$1 and P$\sp\prime$123 arm-type sites and to from attL intasomes, (2) for negative dominance in vitro, (3) for the type I topoisomerase activity, and (4) for the ability to resolve recombination intermediates. I found that (1) residues in a stretch of 88 amino acids in the middle of the protein may be involved in Int-Int interactions, (2) a region around Arg212 is part of the active site, (3) residues in the carboxyl terminal play a role in enhancing Int binding to its arm-type sites, possibly by interacting with the small amino terminal region that is responsible for specific recognition of the arm-type sites, and (4) residues at the very carboxyl end of the protein may be involved in modulating the cleavage or religation activities of the protein."

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Han, Yiping Weng

Contributors dc:contributor

• Gardner, Jeffrey F.

• Biology, Genetics
• Biology, Microbiology

Statement dc:rights

• Copyright 1993 Han, Yiping Weng

Language dc:language

eng

Identifier

AAI9329051
(UMI)AAI9329051

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19633