{"id":391,"date":"2013-02-04T22:02:16","date_gmt":"2013-02-04T22:02:16","guid":{"rendered":"http:\/\/research.chemistry.ohio-state.edu\/musier\/?page_id=391"},"modified":"2017-06-05T22:37:41","modified_gmt":"2017-06-06T02:37:41","slug":"dr-william-cantara","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/dr-william-cantara\/","title":{"rendered":"Dr. William Cantara"},"content":{"rendered":"

\"\"<\/a><\/p>\n

Email: cantara.2@osu.edu<\/span><\/p>\n

BACKGROUND<\/strong><\/span>
\n B.S. Biochemistry and Physics: Juniata College, 2001-2005<\/span>
\n QC Chemist: Croda Inc., 2005-2006<\/span>
\n Biosensor Scientist: Conductive Technologies Inc., 2006-2007<\/span>
\n Ph.D. Molecular & Structural Biochemistry: NC State Univ., 2007-2012<\/span>
\n Postdoc. Researcher: Chemistry & Biochemistry, The Ohio State Univ., 2012-present<\/span>
\n Pelotonia Postdoctoral Fellow: The Ohio State University, 2013-2015<\/span><\/p>\n

RESEARCH INTERESTS<\/strong><\/span>
\n Structural mechanisms of retroviral packaging<\/strong><\/em><\/span>
\n The 5\u2032 untranslated region (5\u2032UTR) of retroviral genomic RNA is highly structured and plays roles in many aspects of replication including promoting reverse transcription, enhancing viral RNA transcription and translation, directing primer annealing, and regulating viral packaging. Therefore, a complete understanding of the molecular mechanisms driving retroviral replication hinges on our ability to structurally characterize functional domains within 5\u2032UTR and their interactions with essential host and viral factors. We are developing methods to solve structures of large RNAs and RNA:protein complexes in solution using a combination of careful sample preparation and optimization, solution scattering techniques and computational modeling to decipher the structural underpinnings of 5\u2032UTR function in two clinically relevant retroviruses, HIV-1 (the virus that causes AIDS) and HTLV-1 (the virus that causes human T-lymphotropic leukemia).<\/span><\/p>\n

Modeling substrate specificity in aminoacyl-tRNA editing proteins<\/strong><\/em><\/span>
\n High fidelity in ribosome-mediated protein synthesis is predicated on covalent attachment of a cognate amino acid onto the correct set of tRNA isoacceptors. Aminoacyl-tRNA synthetases are responsible for this function; however, many are error prone due to similarities in size, shape and physicochemical properties between different amino acids. Recently, our lab and others have identified freestanding editing proteins able to alleviate these errors through post-transfer editing. Currently, it is unclear how these editing proteins distinguish between cognate and non-cognate aminoacyl-tRNAs. Using biochemical data collected in our lab, I am using computational techniques to understand substrate specificity in these proteins and identify potential catalytic mechanisms.<\/span><\/p>\n

CURRENT PUBLICATION LIST<\/strong><\/span><\/p>\n

10. *Cantara, W. A., *Hatterschide, J., Musier-Forsyth, K.\u00a0\u00a0(2017). RiboCAT: a new capillary electrophoresis data analysis tool for nucleic acid probing. RNA<\/em> 23(2), 240-249.<\/span><\/p>\n

9. Cantara, W. A., Olson, E. D., Musier-Forsyth, K.\u00a0\u00a0(2017). Analysis of RNA structure using small-angle X-ray scattering. Methods<\/em> 113, 46-55.<\/span><\/p>\n

8. *Olson, E. D., *Cantara, W. A., Musier-Forsyth, K.\u00a0\u00a0(2015). New structure sheds light on selective HIV-1 genomic RNA packaging. Viruses<\/em> 7(8), 4826-4835.<\/span><\/p>\n

7.\u00a0*Cantara, W. A., *Olson, E. D. & Musier-Forsyth, K. (2014). Progress and outlook in structural biology of large viral RNAs. Virus Res<\/em> 193, 24-38.<\/span><\/p>\n

6.\u00a0*Jones, C. P., *Cantara, W. A., Olson, E. D. & Musier-Forsyth, K. (2014). Small-angle X-ray scattering-derived structure of the HIV-1 5′ UTR reveals 3D tRNA mimicry. Proc Natl Acad Sci U S A<\/em> 111, 3395-3400.<\/span><\/p>\n

5. Cantara, W. A., Murphy, F. V., Demirci, H. & Agris, P. F. (2013). Expanded use of sense codons is regulated by modified cytidines in tRNA. Proc Natl Acad Sci USA<\/em> 110, 10964-9.<\/span><\/p>\n

4. Vendeix, F. A., Murphy, F. V., Cantara, W. A., Leszczynska, G., Gustilo, E. M., Sproat, B., Malkiewicz, A. & Agris, P. F. (2012). Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism. J Mol Biol<\/em> 416, 467-85. Featured Article<\/span><\/p>\n

3. *Cantara, W. A., *Bilbille, Y., Kim, J., Kaiser, R., Leszczynska, G., Malkiewicz, A. & Agris, P. F. (2012). Modifications modulate anticodon loop dynamics and codon recognition of E. coli tRNA(Arg1,2). J Mol Biol<\/em> 416, 579-97.<\/span><\/p>\n

2. Cantara, W. A., Crain, P. F., Rozenski, J., McCloskey, J. A., Harris, K. A., Zhang, X., Vendeix, F. A., Fabris, D. & Agris, P. F. (2011). The RNA Modification Database, RNAMDB: 2011 update. Nucleic Acids Res<\/em> 39, D195-201.<\/span><\/p>\n

1. Lusic, H., Gustilo, E. M., Vendeix, F. A., Kaiser, R., Delaney, M. O., Graham, W. D., Moye, V. A., Cantara, W. A., Agris, P. F. & Deiters, A. (2008). Synthesis and investigation of the 5-formylcytidine modified, anticodon stem and loop of the human mitochondrial tRNAMet. Nucleic Acids Res<\/em> 36, 6548-57.<\/span><\/p>\n

* Authors contributed equally.<\/span><\/p>\n","protected":false},"excerpt":{"rendered":"

Email: cantara.2@osu.edu BACKGROUND B.S. Biochemistry and Physics: Juniata College, 2001-2005 QC Chemist: Croda Inc., 2005-2006 Biosensor Scientist: Conductive Technologies Inc., 2006-2007 Ph.D. Molecular & Structural Biochemistry: NC State Univ., 2007-2012 Postdoc. Researcher: Chemistry & Biochemistry, The Ohio State Univ., 2012-present<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-391","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/pages\/391","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/comments?post=391"}],"version-history":[{"count":6,"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/pages\/391\/revisions"}],"predecessor-version":[{"id":1148,"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/pages\/391\/revisions\/1148"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/musier-forsyth.1\/wp-json\/wp\/v2\/media?parent=391"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}