Dr. Jana Villemain

  • Associate Professor

    Office: 237A Weyandt Hall
    Phone: 724-357-2180 
    Email: J.Villemain@iup.edu

    Office Hours

    T: 9:00–11:00 a.m.
    W: 11:00 a.m.–12:20 p.m.
    R: 9:00 a.m.–11:00 a.m.


    BS – Southwestern University
    PhD – Texas A&M University   
    Postdoctoral Fellowship – University of Texas Health Science Center at San Antonio        




    CHEM 101/102 — College Chemistry I/II
    BIOC 301/302 — Foundations of Biochemistry I/Advanced Biochemistry
    BIOC 311/312 — Biochemistry Lab I/II
    CHEM 351 — Biochemistry
    BIOC 480/490 — Biochemistry Seminar I/II
    BIOC 481 — Special Topics in Biochemistry

    Research Interests

    Protein 3D Structure and how it relates to protein function 
    Intrinsically Unstructured Proteins their Regulatory Role in Cell Function
    Fluorescence Microscopy of Proteins

    There are two primary areas of focus in my lab:  

    1. ville0Investigating the C-terminal domain of the eukaryotic Srs2 helicase, a regulatory protein in the DNA double-stranded break repair pathway using fluorescence spectroscopic techniques: The C-terminal region of this protein shares features with intrinsically unstructured proteins which likely contributes to its ability to interact with different proteins in the cell to carry out its role.
    2. Monitoring protein traffic in yeast under different cellular conditions: We can follow the time-dependent localization of fluorescently labeled proteins and dyes using the state-of-the-art IMIC fluorescence confocal microscope vile1recently acquired through the joint efforts of faculty from the Biology, Chemistry, and Physics departments. One goal is to develop fluorescence confocal microscopy studies to include in future undergraduate biochemistry lab courses.

    We use a range of techniques in our studies such molecular biology, bacterial and yeast cell culture, chromatography, spectroscopy, and bioinformatics resources in our studies.

    Select Publications

    Wise, Christopher and Villemain, J.L 2015.  Post-Translational Regulation of Membrane Bound Proteins. 29th Annual ACS Regional Symposium, Duquesne University. 

    Limbacher, M. and Villemain, J.L. 2014. Monitoring Fluorescence Changes of Tryptophan in Bovine Serum Albumin.  ACS Central and Regional Meeting, Pittsburgh.

    Shaley, K. and Villemain, J.L . 2012. Cloning, expression and purification of two C-terminal fragments of S. cerevisiae Srs2 helicase to study structural changes upon binding to Rad 51 protein. Pennsylvania Academy of Sciences Annual Meeting. 

    Shaley, K., and Villemain, J.L. 2011. Essential Structural Characteristics of the Saccharomyces cerevisiae Srs2 Helicase C-terminal Region to Its Multifaceted Role in Mediating Homologous Recombination Events. Pennsylvania Academy of Sciences Annual Meeting.

    Krejci, L., Macris M, Li Y, Van Komen, Villemain, J.L ., Ellenberger T, Klein H,  Sung, P. 2004.  Role of ATP Hydrolysis in the Anti-Recombinase Function of Activity of the Saccharomyces cerevisiae Srs2 Protein. J.Biol.Chem., 279(22), 23193-23199.

    Krejci, L., Van Komen, S., Li, Y., Villemain, J . , Reddy, M.S., Klein, H., Ellenberger, T., and Sung, P. 2003.  DNA helicase Srs2 disrupts the Rad51 presynaptic filament.  Nature, 423(6937), 305-309.

    Villemain, J.L . , Ma, Y., Giedroc, D.P., and Morrical, S.W. 2000. Functional Activities of N-terminal Domain Mutants of Gene 32 Protein: UvsX-catalyzed Homologous Pairing and Strand Displacement DNA Synthesis, J.Biol.Chem. 275, 31496-31504.

    Huang, J.B., Villemain, J.L . Padilla, R., and Sousa, R. 1999. Mechanisms by which T7 Lysozyme Specifically Regulates T7 RNA Polymerase during Different Phases of Transcription. J.Mol.Biol., 293, 457-475.

    Villemain, J.L. and Sousa, R. 1998. Specificity in Transcriptional Regulation in the Absence of Specific DNA Binding Sites:  The Case of T7 Lysozyme.  J.Mol.Biol. 278, 573-583.

    Villemain, J.L., Guajardo, R., and Sousa, R. 1997.  Role of Open Complex Stability in kinetic Promoter Selection by T7 RNA Polymerase, J.Mol.Biol. 273, 958-977.