At Emory, Jack studied how the ribosome avoids frameshift errors while reading the genetic code and also determined how a class of RNA methyltransferases recognize and methylate rRNA to confer resistance to aminoglycoside antibiotics.
At UA, the Dunkle Research Group is studying the specificity mechanisms of erythromycin resistance rRNA methyltransferases a clinically important antibiotic resistance determinant, the structure and function of proteins in the Suf Fe-S biosynthesis pathway and the specificity and interference mechanisms of CRISPR-Cas10.
Research Projects:
- Structure and mechanism of erythromycin resistance methyltransferases
- Mechanisms and regulation of CRISPR-Cas interference
- Structural biology of sulfur mobilization
Subject Area: Biochemistry.
Current Research
- Structure and mechanism of RNA modification enzymes, RNA-protein interactions, X-ray crystallography
- Methyltransferases that modify 23S ribosomal RNA to initiate antibiotic resistance
- 6-methyl adenosine containing messenger RNA.