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Raven H. Huang Associate Professor of Biochemistry, Chemistry, and Biophysics Ph.D. 1995, University of Washington Functional and structural characterization of protein enzymes involved in RNA modification and editing, site-specific RNA cleavage, and RNA repair. Raven H. Huang 411 RAL, MC-712 600 S. Mathews Urbana, IL 61801 217-333-3967

The major research in our laboratory focuses on studies of RNA-protein interaction. We are particularly interested in protein enzymes acting on RNA. Using integrated approaches of chemical biology, biochemistry, and structural biology, we strive to provide insight into RNA substrate recognition and reaction mechanisms of the protein enzymes. The research can further be divided into three specific areas that are related to one another.

RNA Modification and Editing. Various RNAs, tRNA in particular, experience post-transcriptional modifications. To date, more than 100 modified nucleotides have been found in RNA. These modifications are important for the biological functions of RNAs. We are interested in mechanistic studies of RNA-modifying enzymes, especially those enzymes involved in hypermodifications near the anticodon of tRNA. In addition, enzymes involved in RNA and DNA editing are also the focus of our study.

RNA Cleavage. Protein synthesis is fundamental to living cells. Therefore, it is a main target of various toxins for cell killing. One strategy employed by some bacteria and viruses for cell killing is to cleave essential RNAs (rRNAs, tRNAs, and mRNAs) involved in protein translation, carried out by a class of toxins called ribotoxins. Our research focuses on discovery, biochemical and structural characterization of ribotoxins that target tRNAs.

RNA Repair. To prevent cell from killing, organisms employ enzymes to repair the damaged RNA cleaved by ribotoxins. Recently, we discovered a bacterial RNA repair system composed of two bacterial proteins Pnkp and Hen1. The novelty of the bacterial repair system is that, in addition to restore the ribotoxin-cleaved RNA to its original form, bacterial Hen1 adds a methyl group at the repair junction to protect the repaired RNA against further ribotoxin attack. Thus, the repaired RNA is "better than new".