JACEK GAERTIG

Professor
Ph.D., 1989
Warsaw University, Poland

RESEARCH

The ability of eukaryotic cells to adopt variable shapes, to move in different directions, or to distribute cell components within the cytoplasm is controlled by a network of filaments: the cytoskeleton. Microtubules are the major type of cytoskeletal filaments, consisting of linear polymers of tubulin proteins. Microtubules form a cytoplasmic network which provides intracellular tracks for organellar transport performed by molecular motors (such a kinesins and dyneins). Furthermore, microtubules provide an internal structural support for many complex organelles such as the centrosomes, basal bodies, mitotic spindle, cilia and flagella.

Our model organism, the ciliate Tetrahymena thermophila, labelled by two monoclonal antibodies: on which recognized polyglycylated tubulin (green) and another which recognizes beta-tubulin (red).

We are studying an unicellular organism, the ciliate Tetrahymena thermophila, which assemble at least 17 distinct microtubular structures in a single cell. Our goal is to determine how specific types of microtubular organelles are assembled and maintained. We use cell biological, biochemical and molecular genetic approaches. In particular, we exploit an approach of genetic transformation of Tetrahymena, which allows us to determine the function of a cloned cytoskeletal protein gene by performing a "gene knockout" in vivo. Current research projects include: 1) identification of molecular domains of tubulin proteins involved in adaptation of microtubules to specific functions, with particular emphasis on the role of post-translational tubulin modifications like acetylation, polyglycylation and polyglutamylation; 2) identification of tubulin domains involved in binding of drugs commonly used in cancer chemotherapy like paclitaxel; 2) studies on proteins involved in assembly of microtubular organelles; currently we study the Tetrahymena homologs of kinesin II, a conserved motor protein, involved in assembly of cilia, 4) we explore the potential of Tetrahymena as a vehicle for expression of foreign proteins of biotechnological importance on the cell surface, including the surface antigens of parasitic protists.

CONTACT INFORMATION
(706) 542-3409, jgaertig@cb.uga.edu
SEE ALSO
Gaertig Lab Page
Biomedical & Health Sciences Institute
NSF Press Release --Researchers Identify Proteins that Direct Intracellular Transport and Locomotion

SUPPORT STAFF

Dave Suryavanshi Wloga

NAME POSITION E-MAIL
Drashti Dave Grad Student drashti@uga.edu
Swati Suryavanshi Grad Student swati@uga.edu
Dorota Wloga Post Doc dwloga@uga.edu

REPRESENTATIVE PUBLICATIONS

Gaertig, J. and M.A. Gorovsky. 1992. "Efficient mass transformation of Tetrahymena thermophila by electroporation of conjugants." Proc. Natl. Acad. Sci. USA 89: 9196-9200.

Gaertig, J., T.H. Thatcher, K.E. McGrath, R. Callahan, and M.A. Gorovsky. 1993. "Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta- tubulin." Cell Motility Cytoskeleton 25: 243-253.

Gaertig, J., T.H. Thatcher, L. Gu, and M.A. Gorovsky. 1994. "Electroporation-mediated replacement of a positively and negatively selectable beta-tubulin gene in Tetrahymena thermophila." Proc. Natl. Acad. Sci. USA 91 4549-4553.

Gaertig, J., L. Gu, B. Hai, and M.A. Gorovsky. 1994. "High frequency vector-mediated transformation and gene replacement in Tetrahymena." Nucleic Acids Res. 22: 5391-5398.

Gaertig, J., M.A. Cruz, J. Bowen, L. Gu, and M.A. Gorovsky. 1995. "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila." J. Cell Biol. 129: 1301-1310.

Gaertig, J., Y. Gao, T.G. Clark, H.W. Dickerson. 1999. "Surface display of a parasite antigen in the ciliate. Tetrahymena thermophila." Nature-Biotechnology 17: 462-465.

Brown, J., C. Marsala, R. Kosoy, J. Gaertig. 1999. "Kinesin-II is preferentially targeted to assembling cilia and is required for ciliogenesis and normal cytokinesis in Tetrahymena." Mol. Biol. Cell. 10, 3081-3096.

Brown, J., C. Hardin, and J. Gaertig. 1999. "Rotokinesis, a novel phenomenon of cell locomotion-assisted cytokinesis in the ciliate Tetrahymena thermophila." Cell Biol. Inter. 23, 841-848.

Gaertig, J. 2000. "Molecular mechanisms of microtubular organelle assembly in Tetrahymena." J. Eukar. Microb. 47: 185-190.

Xia, L., B. Hai, Y. Gao, D. Burnette, R. Thazhath, J. Duan, M.H. Br, N. Levilliers, M.A. Gorovsky, and J. Gaertig. 2000. "Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila." J. Cell. Biol. 149: 1097-1106.

Gaertig, J., and E. Cole. 2000. "The role of cortical geometry in nuclear development in Tetrahymena thermophila." J. Eukar. Microb. 47:590-596.

Clark, T.G., Y. Gao, J. Gaertig, X. Wang, and W. Cheng. 2001. "The I-antigens of Ichthyopthirius multifiiis are GPI-anchored." J. Eukar. Microb. 48: 332-337.

Thazhath R., C. Liu, and J. Gaertig. 2002. "Polyglycylation domain of b-tubulin maintains axonemal architecture and controls progression of cytokinesis in Tetrahymena." Nature Cell Biol. 4: 256-259.

Shang, Y., X. Song, J. Bowen, Y. Gao, J. Gaertig, and M.A. Gorovsky. 2002. "A robust inducible-repressible promoter greatly facilitates somatic and germline gene knockouts, conditional expression and overexpression of homologous and heterologous genes in Tetrahymena thermophila." P.N.A.S. USA 99: 3734-3739.

Brown, J.M., Fine. N.A., Pandiyan G., Thazhath, R. and Gaertig J. 2003. "Hypoxia regulates assembly of cilia in suppressors of Tetrahymena lacking an intraflagellar transport subunit gene." Mol. Biol. Cell. 14: 3192-3207.

Thazhath, R., Jerka-Dziadosz, M., I. D., Duan, J.,.Wloga. D., Gorovsky, M.A., Frankel, J., and Gaertig, J. 2004. "Cell context-specific effects of the Beta-tubulin glycylation domain on assembly and size of microtubular organelles." Mol. Biol. Cell 15: 4136-4147.

Redeker V., Levilliers N., Vinolo E., Rossier J., Jaillard D., Burnette D., Gaertig J., M.H., Bre. 2005. "Tubulin polymodification deficiencies reveal a crosstalk between the C-termini of Alpha- and Beta-tubulin and affect the intraciliary matrix in Tetrahymena. J. Biol. Chem. 280: 596-606.

Janke, C., Rogowski K., Wloga, D., Regnard,C., Kajava, AV., Strub, J-M., Temurak, N., van Dijk,J., Boucher, D., van Dorsselar, A., Suryavanshi, S., Gaertig, J., and Edde B. (2005). Tubulin polyglutamylase enzymes are members of the TTL domain protein family. Science. 308: 1758-1762

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