2026-09-21T19:50:15Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/86685 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Gardner, Jeffrey F. Dichiara, Jeanne M. 2015-09-28T15:17:25Z 2015-09-28T15:17:25Z 10000-01-01 2006 2006 The excision mechanism of CTnDOT is more complicated than any system studied to date. Excision requires multiple accessory proteins. Exc is one protein required for excision, however, its function is unknown. In an attempt to determine a role for Exc, the native wild type Exc protein was purified. These studies indicated that Exc might interact with IntDOT during excision, as determined by electrophoretic mobility shift assays. Further studies of Exc are warranted to answer the many questions that still remain about its function. Made available in DSpace on 2015-09-28T15:17:25Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3242833.pdf: 4334127 bytes, checksum: f50ddae67fcf513bedd329a2f7c708ab (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 87966 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 155 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/86685 (MiAaPQ)AAI3242833 eng Biology, Microbiology DNA -Protein Interactions in the CTnDOT Excisive Intasome text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.