2026-09-22T07:12:03Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84842 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gumport, Richard I. Mattis, Aras Nikodemas 2015-09-25T22:28:09Z 2015-09-25T22:28:09Z 10000-01-01 2007 2007 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. Made available in DSpace on 2015-09-25T22:28:09Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3290313.pdf: 3820598 bytes, checksum: e7bdab6cc1d17c376b022468e65784c4 (MD5) Previous issue date: 2007 Embargo set by: Seth Robbins for item 86123 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 136 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007. http://hdl.handle.net/2142/84842 (MiAaPQ)AAI3290313 eng Chemistry, Biochemistry The P22 Xis Protein: Regulation of Bacteriophage P22 Site -Specific Recombination text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.