Yury Polikanov, PhD
Building & Room:
900 S. Ashland Ave.
Office Phone Voice:
The ultimate goal of our laboratory is to be among the most successful and respected in the field of structural biology. We strive to be recognized for the importance of the research that we do, and also for being open, collegial and fair. We create a learning environment for training of next-generation scientists through our teamwork and collaborations with other researchers in the area across the globe. We believe that the true power of collaboration lies in the diversity of skills, knowledge and expertise, which can be applied to solving a particular problem. Altogether we know a lot and can do a lot, but this knowledge and skills are usually scattered between multiple heads and hands. Therefore, our mission is to bring them altogether and turn our science into exciting dialog (or interview) with mother-nature.
About Dr. Polikanov's Research
Our current research at UIC focuses on the ribosome, a complex molecular machine that is responsible for synthesizing proteins which are the essential building blocks of all living organisms. It is by the action of these ribosomes that the blueprint of life encoded in the DNA is translated into proteins that control every aspect of a living organism at a chemical level. The process of protein synthesis is called translation because ribosome interprets the language of nucleotides in genes into the language of amino acids in the proteins. There are tens and thousands of proteins in our body performing important functions like immune response to pathogens, regulation of heart beat, monitoring blood glucose levels, allowing oxygen absorption in the lungs, and neurotransmission, which are all made by the ribosomes. Hence the process of “protein translation” performed by the ribosome is critical for sustaining life. The principles of ribosome organization and functioning are fundamentally similar between all living organisms, however nearly 3 billion years of independent evolution made our ribosomes slightly different from the ones found in bacteria. Because of these differences, it is possible for some natural compounds - antibiotics - to selectively inhibit ribosomes of pathogenic microorganisms (bacteria), and thereby kill them, with no effect on us (humans). Ribosome inhibitors are among the most successful antimicrobial drugs and constitute more than 50% of all medicines used to treat infections in clinic. However, quick development of resistance to the existing antibiotics by pathogenic microorganisms demands a constant search for new antibiotics and represents a major health care threat in the United States and across the globe. It has been the long-term scientific focus of many laboratories to tackle this recurring problem and the Ribosome Structural Studies are at the forefront of addressing this very issue.
In particular, we are focused on studies of structural aspects of protein synthesis and the mechanisms of action of ribosome-targeting antibiotics. Our vision is that our research will facilitate the development of next-generation antimicrobial compounds, as well as clinical approaches to prevent acquisition of drug resistance by clinical pathogens. We use X-ray crystallography techniques to determine nearly atomic resolution structures of various inhibitors bound to their target - the ribosome. This allows us to understand how ribosome-targetting antibiotics work and how they could be improved.
We are also focused on the fundamental understanding of how multiple elements of the ribosome function together during protein synthesis and what are their individual roles in this process at the molecular level. To this end, we determine structures of the ribosome in complex with its natural ligands, such as different translation protein factors and RNA molecules. One particular direction of our current research is to study one fundamental aspect of ribosome functioning termed “ribosome hibernation” and its link to acquired drug resistance in pathogenic bacteria. When bacteria actively grow and divide, their ribosomes are very efficient protein factories which are constantly synthesizing new proteins to maintain the vital functions. However, under certain conditions, especially when there are not enough nutrients, bacteria slow down protein synthesis and convert their ribosomes into inactive, yet stable forms. This process of inactivation is called “ribosome hibernation” and is mediated by the hibernation factors, which bind to the ribosomes and turn off protein synthesis in a bacterial cell. Antibiotics directly target the actively working ribosomes, but obviously are useless in targeting inactive hibernating ribosomes. Therefore, just by making their ribosomes inactive, pathogenic bacteria can escape the action of antibiotics, ultimately leading to drug resistance. We wish to understand how ribosome hibernation is linked to the acquisition of drug resistance in pathogenic bacteria. This can help in establishing a therapeutic procedure for prevention of ribosome hibernation that can be used as a remedy against development of multiple-drug resistance in pathogens.
(Complete list of publications on Google Scholar)
- Polikanov YS, Starosta AL, Juette MF, Altman RB, Terry DS, Lu W, Burnett BJ, Dinos G, Reynolds K, Blanchard SC, Steitz TA, and Wilson DN. (2015) Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A. Molecular Cell 58(5): 832-844.
- Polikanov YS, Melnikov SV, Söll D, and Steitz TA. (2015) Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly. Nature Structural & Molecular Biology 22(4): 342-344.
- Polikanov YS, Osterman IA, Szal T, Tashlitsky VN, Serebryakova MV, Kusochek P, Bulkley D, Malanicheva IA, Efimenko TA, Efremenkova OV, Konevega AL, Shaw KJ, Bogdanov AA, Rodnina MV, Dontsova OA, Mankin AS, Steitz TA, and Sergiev PV. (2014) Amicoumacin A inhibits translation by stabilizing mRNA interaction with the ribosome. Molecular Cell 56(4): 531-540.
- Polikanov YS, Szal T, Jiang F, Gupta P, Matsuda R, Shiozuka M, Steitz TA, Vázquez-Laslop N, and Mankin AS. (2014) Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA.Molecular Cell 56(4): 541-550.
- Polikanov YS, Steitz TA, and Innis CA. (2014) A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome. Nature Structural & Molecular Biology 21(9): 787-793. Selected for cover image.
- Polikanov YS, Blaha GM, and Steitz TA. (2012) How hibernation factors RMF, HPF, and YfiA turn off protein synthesis. Science 336(6083): 915-918.
- Bulkley D, Brandi L, Polikanov YS, Fabbretti A, O’Connor M, Gualerzi CO, and Steitz TA. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Reports S2211-1247(13): 00782-1.
- Blaha GM*, Polikanov YS*, and Steitz TA. (2012) Elements of ribosomal drug resistance and specificity. Current Opinion in Structural Biology 22(6): 750- 758.
Postdoctoral Training , Yale University 2015
PhD, University of Medicine and Dentistry of New Jersey/Rutgers University 2008
MS, Lomonosov Moscow State University 2004
BS, Lomonosov Moscow State University 2004