DNA Transactions at an Atomic Level

The genetic information encoded within DNA is copied, maintained, and decoded by protein machines. Our laboratory uses X-ray crystallography and other high-resolution structural and biochemical approaches to investigate the molecular details of how these proteins repair damaged DNA and carry out DNA synthesis.

Featured Articles

Parsons et al (2016) J.Am.Chem.Soc., 138: 11485

Mullins et al (2015) Nature, 527: 254     News & Views

In the News

New NIH grant to study replication fork repair

Vanderbilt story on Elwood's paper

Diana's work on HLTF described in VUMC Reporter

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  • Time-resolved crystallography to monitor base excision repair by DNA glycosylases
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  • HLTF's ancient HIRAN domain binds 3' DNA ends to drive replication fork reversal
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  • Bacterial AlkD is the first glycosylase discovered to repair a bulky lesions like the natural product yatakemycin
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  • How do DNA repair enzymes search the genome for chemical damage?

  • How are stalled replication forks repaired?

  • SMARCAL1 HARP domain is important for reversal of stalled forks
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  • HEAT repeats have emerged as an important nucleic acid binding architecture

  • Base flipping is not a prerequisite for excision repair by DNA glycosylases
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  • CH-π interactions important for catalysis of base excision by DNA glycosylase AlkD
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  • Crystals used to determine the atomic structures of a protein-DNA complex

  • X-ray diffraction image from a protein crystal

  • Building the atomic structure of a protein-DNA complex into experimental electron density from X-ray diffraction data

  • NMR chemical shift perturbation to monitor protein structural changes induced by DNA binding
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  • Structural studies of the vertebrate replisome
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  • E. coli AidB is a DNA binding protein involved in the bacterial adaptive response to alkylating agents
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