Contact
Graeme L. Conn, Ph.D.
Associate Professor
Department of Biochemistry
O. Wayne Rollins Rsch. Center
1510 Clifton Rd. NE
Atlanta, GA 30322

4135 Office
4178 Lab
404.727.5965 (Office tel.)
404.712.0058 (Lab tel.)
404.727.2738 (Fax)
gconn@emory.edu

ORCiD
Research Gate

Conn Lab Research

Our lab uses a broad array of biochemical, structural biology and other state-of-the-art approaches to dissect the structures and functions of biomedically important RNA molecules and their protein binding partners. Current topics include: 

Non-coding RNA-mediated regulation of host cell innate immune proteins

Our lab has long-standing interests in the structure and activity of viral non-coding RNAs, such as Adenovirus VA RNAI – an essential, pro-viral RNA best known for inhibition of the double-stranded (ds)RNA-activated protein kinase (PKR). More recently, we have begun new studies that aim to determine which features of simple dsRNAs and larger, complex viral and cellular non-coding RNAs are important for regulation of a second innate immune protein, oligoadenylate synthetase 1 (OAS1).
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RNA modification and bacterial antibiotic resistance

Rising antibiotic resistance among human pathogenic bacteria is a major contemporary healthcare problem. We are studying several examples of how bacterial antibiotic resistance can arise through chemical modification (methylation) of the ribosomal RNA (rRNA) antibiotic binding site. This mechanism of resistance is predominant among antibiotic-producing bacteria, but has also more recently been more recently identified as an acquired form of resistance in diverse human pathogens. Such modifications of the drug binding site can confer exceptionally high-level resistance and broad specificity to a given class of antibiotics, making them a significant potential new threat.
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Molecular mechanisms of RNA and protein methylations in biology and disease

In collaboration with other labs at Emory and elsewhere, we are investigating the molecular mechanisms and biological impacts of other RNA and protein modification processes.
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