Structural Studies of Hmg-D-Dna Interactions

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Murphy, Frank Vincent, IV

Contributors dc:contributor

• Mair E.A.Churchill

• Biology, Molecular

Language dc:language

eng

Identifier

(MiAaPQ)AAI9971143

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84913