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https://hdl.handle.net/2142/84913
Description
Title
Structural Studies of Hmg-D-Dna Interactions
Author(s)
Murphy, Frank Vincent, IV
Issue Date
2000
Doctoral Committee Chair(s)
Mair E.A.Churchill
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
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.
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