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Title:Structural Studies of Hmg-D-Dna Interactions
Author(s):Murphy, Frank Vincent, IV
Doctoral Committee Chair(s):Mair E.A.Churchill
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Biology, Molecular
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.
Issue Date:2000
Type:Text
Language:English
Description:130 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.
URI:http://hdl.handle.net/2142/84913
Other Identifier(s):(MiAaPQ)AAI9971143
Date Available in IDEALS:2015-09-25
Date Deposited:2000


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