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:

  • 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]
  • Margolin W (2006) Gliding motility: anticipating the next move with a molecular clock. Curr Biol 16:85 [abstract]
  • Margolin W (2006) Bacterial division: Another way to box in the ring. Curr Biol 16:881 [abstract]
  • Margolin W (2005) Bacterial mitosis: Actin in a new role at the origin. Curr Biol 15:259 [abstract]
  • Margolin W (2005) FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6:862 [abstract]
  • Geissler B, and Margolin W (2005) Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK. Mol Microbiol 58:596 [abstract]
  • Corbin BD, Geissler B, Sadasivam M, Margolin W (2004) Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J Bacteriol 186:7736 [abstract]
  • Margolin W, Bernander R (2004) How do prokaryotic cells cycle? Curr Biol 14:768 [abstract]
  • Thanedar S, Margolin W (2004) FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr Biol 2004 14:1167 [abstract]
  • Margolin W (2004) Catching some Zs: a new protein for spatial regulation of bacterial cytokinesis. Cell 117:850 [abstract]
  • Sun Q, Margolin W (2004) Effects of perturbing nucleoid structure on nucleoid occlusion-mediated toporegulation of FtsZ ring assembly. J Bacteriol 186:3951 [abstract]
  • Margolin W (2004) Bacterial shape: concave coiled coils curve Caulobacter. Curr Biol 14:242 [abstract]
  • Tan XX, Rose K, Margolin W, Chen Y (2004) DNA enzyme generated by a novel single-stranded DNA expression vector inhibits expression of the essential bacterial cell division gene ftsZ. Biochemistry 43:1111 [abstract]
  • Gilson PR, Yu XC, Hereld D, Barth C, Savage A, Kiefel BR, Lay S, Fisher PR, Margolin W, Beech PL (2003) Two Dictyostelium orthologs of the prokaryotic cel division protein FtsZ localize to mitochondria and are required for the maintenance of normal mitochondrial morphology. Eukaryot Cell 2:1315 [abstract]
  • Margolin W (2003) Bacterial shape: growing off this mortal coil. Curr Biol 13:705 [abstract]
  • Mileykovskaya E, Fishov I, Fu X, Corbin BD, Margolin W, Dowhan W (2003) Effects of phospholipid composition on MinD-membrane interactions in vitro and in vivo. J Biol Chem 278:22193 [abstract]
  • Geissler B, Elraheb D, Margolin W (2003) A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc Natl Acad Sci USA 100:4197 [abstract]
  • Margolin W (2003) Bacterial division: the fellowship of the ring. Curr Biol 13:R16 [abstract]

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