Jumi A. Shin

faculty_img Academic Title: Associate Professor

Campus: UTM

CSB Appointment: Cross Appointment

Primary Undergraduate Department:
Chemical & Physical Sciences

Graduate Programs:

Titles and Honors:
Premier’s Research Excellence Award
National Science Foundation CAREER Award

Ph.D., California Institute of Technology 1992
A.B. Cum Laude, Harvard University 1986 


Mailing Address
Department of Chemistry
University of Toronto
3359 Mississauga Road
Mississauga, ON L5L 1C6 Canada


Contact Information
TEL: (905) 828-5355, FAX: (905) 838-5425
Email: jumi.shin@utoronto.ca
URL: http://www.utm.utoronto.ca/~shinjumi/


Research Areas
Protein design & engineering
Directed evolution
Artificial transcription factors


Our work uses molecular and cellular biology and biophysical approaches to design small proteins that target DNA sequences important in disease. For example, our 66 amino acid protein ME47 targets the E-box sequence, which is involved in over half of all cancers, and competitively inhibits native transcription factors from binding their DNA targets. ME47 can be used to modulate breast cancer cell growth in mouse models. We also study how continuous exposure to pollutants, like quantum dots, can cause organisms to genetically adapt.



“Guiding principles for a successful multidisciplinary research collaboration.” L. C. Lustig, R. Ponzielli, P. S. Tang, S. Sathiamoorthy, I. Inamoto, J. A. Shin, L. Z. Penn, W. C. W. Chan. Future Science Open Access, March 20, 2015, 1-4.
“The Role of Ligand Density and Size in Mediating Quantum Dot Nuclear Transport.” P. Tang, S. Sathiamoorthy, L. Lustig, R. Ponzielli, I. Inamoto, L. Z. Penn, J. A. Shin, & W. C. W. Chan. Small, 2014, 10, 4182–4192. DOI: 10.1002/smll.201401056. Pubmed ID: 24990622
“Boundaries of the Origin of Replication: Creation of a pET-28a-Derived Vector with p15A Copy Control Allowing Compatible Coexistence with pET Vectors.” S. Sathiamoorthy & J. A. Shin. PLoS ONE, 2012, 7, e47259. doi:10.1371/journal.pone.0047259. Pubmed ID: 23110063
“The bZIP Dimer Localizes at DNA Full-Sites Where Each Basic Region Can Alternately Translocate and Bind to Subsites at the Half-Site.” I. Chan, T. Al-Sarraj, H. S. Shahravan, A. V. Fedorova, & J. A. Shin. Biochemistry, 2012, 51, 6632-6643. Pubmed ID: 22856882
“Forced homodimerization of the Fos leucine zipper in designed bHLHZ-like hybrid proteins MaxbHLH-Fos and ArntbHLH-Fos.” G. Chen, A. T. De Jong, & J. A. Shin. Molecular BioSystems, 2012, 8, 1286-1296. Pubmed ID: 22301802
“Crystal structure of the minimalist Max-E47 protein chimera.” F. Ahmadpour, R. Ghirlando, A. T. De Jong, M. Gloyd, J. A. Shin, & A. Guarne. PLoS ONE, 2012, 7, e32136 (doi:10.1371/journal.pone.0032136). Pubmed ID: 22389683
“FRep: a fluorescent protein-based bioprobe for in vivo detection of protein:DNA interactions.” S. H. Shahravan, I. T. Li, K. Truong, & J. A. Shin. Analytical Chemistry, 2011, 83, 9643-9650. Pubmed ID: 22074380
“Reengineering natural design by rational design and in vivo library selection: the HLH domain in bHLHZ proteins is a unique requirement for DNA-binding function.” J. Xu, A. T. De Jong, H.-K. Chow, G. Chen, C. O. Damaso, A. Schwartz Mittelman, & J. A. Shin. Protein Engineering, Design, & Selection, 2010, 23, 337-346. Pubmed ID: 20086039
“Max-E47, a designed minimalist protein that targets the E-box DNA site in vivo and in vitro.” J. Xu, G. Chen, A. T. De Jong, S. H. Shahravan, & J. A. Shin. Journal of the American Chemical Society, 2009, 131, 7839-7848. Pubmed ID: 19449889
“Hybrids of the bHLH and bZIP Protein Motifs Display Different DNA-Binding Activities in vivo vs. in vitro.” H.-K. Chow, J. Xu, S. H. Shahravan, A. T. De Jong, G. Chen, & J. A. Shin. PLoS ONE, 2008, 3, e3514 (doi:10.1371/journal.pone.0003514). Pubmed ID: 18949049
“AhR/Arnt:XRE interaction: turning false negatives into true positives in the modified yeast one-hybrid assay.” G. Chen & J. A. Shin. Analytical Biochemistry, 2008, 382, 101-106. Pubmed ID: 18722998
“Design of a single plasmid-based modified yeast one-hybrid system for investigation of in vivo protein-protein and protein-DNA interactions.” G. Chen, L. M. DenBoer, & J. A. Shin. BioTechniques, 2008, 45, 295-304. Pubmed ID: 18778253
“The bZIP targets overlapping DNA sub-sites within a half site resulting in increased binding affinities.” I. Chan, H. S. Shahravan, A. V. Fedorova, & J. A. Shin. Biochemistry, 2008, 47, 9646-9652. Pubmed ID: 18702507
“Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag.” H. S. Shahravan, X. Qu, I. Chan, & J. A. Shin. Protein Expression and Purification, 2008, 59, 314-319. Pubmed ID: 18406169
“The GCN4 bZIP Targets Noncognate Gene Regulatory Sequences: Quantitative Investigation of Binding at Full and Half Sites.” I. Chan, A. V. Fedorova, & J. A. Shin. Biochemistry, 2007, 46, 1663-1671. Pubmed ID: 17279629
“The GCN4 bZIP Can Bind to Noncognate Gene Regulatory Sequences.” A. V. Fedorova, I. Chan, & J. A. Shin. Biochimica et Biophysica Acta (Proteins and Proteomics), 2006, 1764, 1252-1259. Pubmed ID: 16784907
“Minimalist Proteins: Design of New Molecular Recognition Scaffolds.” J. A. Shin. Pure and Applied Chemistry, 2004, 76, 1579-1590. Pubmed ID: 19461942
“Sequence-Specific Recognition of DNA by Hydrophobic, Alanine-scanning Mutants of the bZIP Motif Investigated by Fluorescence Anisotropy.” G. H. Bird, A. R. Lajmi, & J. A. Shin. Biopolymers, 2002, 65, 10-20. Pubmed ID: 12209468
“MALDI-TOF Mass Spectrometry Characterization of Hydrophobic Basic Region/Leucine Zipper Proteins.” G. H. Bird & J. A. Shin. Biochimica et Biophysica Acta (Protein Structure & Molecular Enzymology), 2002, 1597, 252-259. Pubmed ID: 12044903
“Manipulation of Temperature to Improve Solubility of Hydrophobic Proteins and Cocrystallization with Matrix for Analysis by MALDI-TOF Mass Spectrometry.” G. H. Bird, A. R. Lajmi, & J. A. Shin. Analytical Chemistry, 2002, 74, 219-225. Pubmed ID: 11795797
“The Contribution of the Methyl Groups on Thymine Bases to Binding Specificity and Affinity by Alanine-rich Mutants of the bZIP Motif.” K. J. Kise Jr. & J. A. Shin. Bioorganic and Medicinal Chemistry, 2001, 9, 2485-2491. Pubmed ID: 11553490
“Short, Hydrophobic, Alanine-based Proteins Based on the bZIP Motif: Overcoming Inclusion Body Formation and Protein Aggregation During Overexpression, Purification, and Renaturation.” A. R. Lajmi, T. R. Wallace, & J. A. Shin. Protein Expression and Purification, 2000, 18, 394-403. Pubmed ID: 10733895
“Minimalist, Alanine-based, Helical Protein Dimers Bind to Specific DNA Sites.” A. R. Lajmi, M. E. Lovrencic, T. R. Wallace, R. R. Thomlinson, & J. A. Shin. Journal of the American Chemical Society, 2000, 122, 5638-5639.
“Specific DNA Binding Peptide-Derivatized Solid Support.” J. A. Shin. Bioorganic and Medicinal Chemistry Letters, 1997, 7, 2367-2372.

“Mechanistic Studies of an Antibody with Chorismate Mutase Activity.” J. A. Shin & D. Hilvert. Bioorganic and Medicinal Chemistry Letters, 1994, 4, 2945-2948.
“Orientation of the Lac Repressor DNA Binding Domain In Complex with the Left Lac Operator Half Site Characterized by Affinity Cleaving.” J. A. Shin, R. H. Ebright, & P. B. Dervan. Nucleic Acids Research, 1991, 19, 5233-5236. Pubmed ID: 1923807
“Cooperative Binding of Oligonucleotides to DNA by Triple Helix Formation: Dimerization via Watson-Crick Hydrogen Bonds.” M. D. Distefano, J. A. Shin, & P. B. Dervan. Journal of the American Chemical Society, 1991, 113, 5901-5902.
“Orientation of the Putative Recognition Helix in the DNA-Binding Domain of Hin Recombinase Complexed with the Hix Site.” D. P. Mack, J. P. Sluka, J. A. Shin, J. H. Griffin, M. I. Simon, & P. B. Dervan. Biochemistry, 1990, 29, 6561-6567. Pubmed ID: 2204416