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Title:The P22 Xis Protein: Regulation of Bacteriophage P22 Site -Specific Recombination
Author(s):Mattis, Aras Nikodemas
Doctoral Committee Chair(s):Gumport, Richard I.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Chemistry, Biochemistry
Abstract:Mutants of P22 Xis were isolated and assayed for excision system in vivo, to quantify their excision activity relative to wild-type Xis. Mutants S18F, R19A, G29S, G29D, A33P, R35C, D37G, S43F, S43P, P44L, L46F, A51T, and A51V were found to be defective in stimulating excision. Additionally, truncation mutants S66Z, K76Z, and D97Z were decreased in function about five-fold. In contrast, truncation mutants Q57Z and a mutant with the first 21 amino acids deleted were completely defective. Substitution mutants at R105, K107, and R109 revealed that this region stimulates the reactaion. A subset of Xis mutants were purified and assayed by EMSA and crosslinking studies. All purified mutants formed multimers by crosslinking, but L15F, K16E, A33P, S43F, and A55T were defective in DNA binding. Furthermore, L46F bound DNA with a weaker affinity but still formed specific complexes.
Issue Date:2007
Type:Text
Language:English
Description:136 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007.
URI:http://hdl.handle.net/2142/84842
Other Identifier(s):(MiAaPQ)AAI3290313
Date Available in IDEALS:2015-09-25
Date Deposited:2007


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