The University of Texas Medical School at Houston
Department of Microbiology and Molecular Genetics

William Margolin, Ph.D.

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  • William Margolin, Ph.D.Professor
  • Department of Microbiology &
    Molecular Genetics
  • University of Texas-Houston Medical School
    6431 Fannin Street, MSB 1.167
    Houston, Texas 77030
  • Telephone: (713) 500-5452
    Laboratory Telephone: (713) 500-5453
    e-mail:william.margolin@uth.tmc.edu

 

Education:

Ph.D., University of Wisconsin, 1989

Postdoctoral Fellow, Stanford University

Research Interests:

Targeting and assembly of the bacterial cell division complex

Cell division, or cytokinesis, is a fundamental requirement for the proliferation of all cells. Cytokinesis is regulated temporally and spatially to insure that daughter cells contain the normal complement of chromosomes. We study the regulation of cell division in bacteria, which enables us to use highly sophisticated genetic approaches. Despite our vast knowledge of prokaryotic biology, we still understand surprisingly little about how bacteria, such as Escherichia coli, divide by binary fission.

One of the cell division proteins we focus on is FtsZ. FtsZ is an abundant protein that, in response to an unknown signal, polymerizes into a ring structure marking the division site and is essential for the initiation of cell division. Other essential proteins, such as FtsA and FtsK, are then recruited to the FtsZ ring and act in a putative complex to complete division. FtsZ is ubiquitous, with homologs in eubacteria, archaea and chloroplasts. Current evidence suggests that FtsZ is essential to define the cell division plane in all non-nucleated cells. What has made working on this protein even more exciting is that FtsZ is structurally and enzymatically similar to tubulin, and probably is tubulin's evolutionary ancestor. FtsZ and tubulin are the building blocks for the FtsZ division ring and microtubules, respectively, which are essential cytoskeletal structures in prokaryotes and eukaryotes. Nevertheless, their functions are quite different: The FtsZ ring helps to form the division septum, whereas microtubules are involved in movement of chromosomes during mitosis.

Our long-term goals are to understand how FtsZ and other cell cycle proteins target precisely to the division site, do so only once per cell division cycle, and achieve the constrictive force necessary for cytokinesis. We are also interested in the diversity of cell division mechanisms among microorganisms.

Selected Publications:

  • Hu, B., Margolin, W., Molineux, I.J., Liu, J. (2013) The bacteriophage T7 virion undergoes extensive structural remodeling during infection. Science. 339:576-579. [abstract]
  • Margolin, W. (2012) The price of tags in localization studies. J. Bacteriol. 194:6369-6371. [abstract]
  • Haeusser, D.P. and Margolin, W. (2012) Bateriophage tubilins: Carrying their own skeleton key. Curr. Biol. 22:639-641. No abstract available.
  • Mileykovskay, E., Margolin, W. (2012) "Cell division" in Eschericia coli and Bacillus subtilis: The Frontiers of Molecular Microbiology Revisited, Yoshito Sadaie and Kouji Matsumoto, eds., Research Signpost Publishing, Kerala, India.
  • Liu, J., Hu, B., Morado, D., Jani, S., Manson, M.D., Margolin, W. (2012) Molecular architecture of chemoreceptor arrays revealed by electron tomography of Escherichia coli minicells. Proc. Natl. Acad. Sci. 109:E1481-1488. [abstract]
  • Juarez, J.R., Margolin, W. (2012) A bacterial actin unites to divide bacterial cells. EMBO J. 31:2235-2236. No abstract available.
  • Wells, V.L., Margolin, W. (2012) A new slant to the Z ring and bacterial cell branch formation. Mol. Microbiol. 84:199-202. [abstract]
  • Busiek, K.K., Eraso, J.M., Wang, Y., Margolin, W. (2012) The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN. J. Bacteriol. 194:1989-2000. [abstract]
  • Busiek, K.K., Margolin, W. (2011) Split decisions: A thaumarchaeon encoding both FtsZ and Cdv cell division proteins chooses Cdv for cytokinesis. Mol. Microbiol. 82:535-538. [abstract]
  • Eraso, J.M., Margolin, W. (2011) Bacterial cell wall: Thinking globally, actin locally. Curr. Biol. 21:R628-630. [abstract]
  • Jiang, H., Si, F., Margolin, W., Sun, S.X. (2011) Mechanical control of bacterial cell shape. Biophys J. 101:327-335. [abstract]
  • Liu, J., Chen, C.Y., Shiomi, D., Niki, H., Margolin, W. (2011) Visualization of bacteriophage P1 infection by cryo-electron tomography of tiny Escherichia coli. Virology. 417:304-311. [abstract]
  • Haeusser, D.P., Margolin, W. (2011) Prokaryotic cytokinesis: Little rings bring big cylindrical things. Curr. Biol. 21:R221-223. [abstract]
  • Hale, C.A., Shiomi, D., Liu, B., Bernhardt, T.G., Margolin, W., Niki, H., de Boer, P.A. (2011) Indentification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds adn bundles FtsZ polymers. J. Bacteriol. 193:1393-1404. [abstract]
  • Beuria, T.K., Margolin, W. (2010) Bacterial cytokinesis: FzIA frizzes FtsZ filaments for fission force. Curr. Biol. 20:R1024-1027. [abstract]
  • Tonthat, NK, Arold, ST, Pickering, B.F., Van Dyke, M.W., Liang, S., Lu, Y., Beuria, T.K., Margolin, W., Schumacher, M.A. (2010) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 30:154-164. [abstract]
  • Juarez JR, Margolin, W. (2010) Changes in the Min oscillation pattern before and after cell birth. J. Bacteriol. 192:4134-4142. [abstract]
  • Margolin, W. (2009) Sculpting the Bacterial Cell. Curr Biol 19:812-822. [abstract]
  • Juarez JR, Margolin, W. (2009) Irresistible curves. EMBO J 28:2147-2148. [abstract]
  • Beuria TK, Mullapudi S, Mileykovskaya E, Sadasivam M, Dowhan W, Margolin, W. (2009) Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA. J Biol Chem 284:14079-14086. [abstract]
  • Mazor S, Regev T, Mileykovskaya E, Margolin, W., Dowhan W, Fishov I (2008) Mutual effects of MinD-membrane interaction: I. Changes in the membrane properties induced by MinD binding. Biochim Biophys Acta 1778:2496-2504. [abstract]
  • Mazor S, Regev T, Mileykovskaya E, Margolin, W., Dowhan W, Fishov I (2008) Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding. Biochim Biophys Acta 1778:2505-2511. [abstract]
  • Letek M, Ordonez E, Vaquera J, Margolin, W., Flardh K, Mateos LM, Gil JA (2008) DivIVA is required for polar growth in the MreB-lacking rod-shaped actinomycete Corynebacterium glutamicum. J Bacteriol 190:3283-3292. [abstract]
  • Shiomi D, Margolin, W. (2008) Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function. Mol Microbiol 67:558-569. [abstract]
  • Shiomi D, Margolin, W. (2007) Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol Microbiol 66:1396-1415. [abstract]
  • Margolin, W. (2007) Bacterial cytoskeleton: not your run-of-the-mill tubulin. Curr Biol 17:633-636. [abstract]
  • Shiomi D, Margolin, W (2007) A sweet sensor for size-conscious bacteria. Cell 130:216-218. [abstract]
  • Bernard CS, Sadasivam M, Shiomi D, Margolin, W. (2007) An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli. Mol Microbiol 64:1289-1305. [abstract]
  • Corbin, BD, Wang Y, Beuria TK, Margolin, W. (2007) Interaction between cell division proteins FtsE and FtsZ. J Bacteriol, 189:3026-35 [abstract]
  • Shiomi D, Margolin, W. (2007) The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli. J Bacteriol 189:236 [abstract]
  • Geissler B, Shiomi D, Margolin, W. (2007) The ftsA* gain of function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153:814 [abstract]
  • Kruse K, Howard M, Margolin, W. (2007) An experimentalist’s guide to modeling of the Min system. Mol Microbiol 63:1279 [abstract]
  • [Search PubMed for more papers by William Margolin]