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oai:www.ideals.illinois.edu:2142/84913 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Mair E.A.Churchill Murphy, Frank Vincent, IV 2015-09-25T22:28:28Z 2015-09-25T22:28:28Z 10000-01-01 2000 2000 HMG-D is a non-sequence-specific non-histone chromosomal protein abundant in early Drosophila embryogenesis. It is a member of the HMG1/2 family of proteins, all of which share the HMG domain, a small DNA-binding structural motif. HMG1/2 proteins interact directly with nucleosomes, modulate chromatin structure, and modulate the activation of gene expression by a number of transcriptional activators. The structure of HMG-D bound to linear duplex DNA shows that the protein distorts the DNA upon binding, forming a tight protein-DNA interface. The structure of the HMG-D-DNA complex is very similar to the complexes of sequence-specific HMG-domain proteins bound to their cognate DNA molecules. However, the structure of HMG1 box A bound to a cisplatin-modified DNA molecule is very different from the nonsequence-specific and sequence-specific HMG-domain protein-DNA complexes. Analysis of the three structures of non-sequence-specific, non-enzymatic protein-DNA complexes determined to date reveals that for minor groove-binding non-sequence-specific proteins, hydrophobic interaction interfaces with base step intercalation and water-mediated hydrogen bonding are the general rule. It is proposed that this will generalize to other such proteins. Made available in DSpace on 2015-09-25T22:28:28Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9971143.pdf: 6992236 bytes, checksum: b504ba4aea9dec4ab1c05fc53ab10235 (MD5) Previous issue date: 2000 Embargo set by: Seth Robbins for item 86194 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 130 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000. http://hdl.handle.net/2142/84913 (MiAaPQ)AAI9971143 eng Biology, Molecular Structural Studies of Hmg-D-Dna Interactions text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.