• Institute of Molecular Biophysics
  • Associate in Research
  • phone: (850) 644-4104
  • diane@rebel.sb.fsu.edu

Since Uzgiris and Kornberg showed that lipid monolayers formed excellent substrates for 2-D crystallization of proteins and macromolecular assemblies. We are using this technique to crystallize cytoskeletal proteins and their complexes. One of these molecules currently being studied is the actin crosslinking protein alpha-actinin. 2-D crystals of alpha-actinin have been formed on positively charged lipid monolayers. In addition, paracrystalline aggregates of F-actin and the complex between F-actin and α-actinin have also been formed on these same lipid monolayers. The technology for formation of 2-D paracrystalline bundles of F-actin on lipid monolayers makes it possible to study additional complexes between F-actin and its crosslinkers which hitherto had formed 3-D gels or bundles. The image to the right was published from Biophys. J. 67, 1976-1983 in 1994.

PUBLICATIONS

  • M. Misra, D. W.Taylor, T. Oliver ; and K. Taylor. Effect of organic anions on the crystallization of the Ca++-ATPase of muscle sarcoplasmic reticulum. Biochim. Biophys. Acta. 1077, 107-118 (1991).
  • K. A. Taylor & D. W. Taylor. Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants. J. Struct. Biol. 108, 140-147 (1992).
  • K. A. Taylor & D. W. Taylor. Projection image of smooth muscle α-actinin from 2-D crystals formed on positively charged lipid layers. J. Mol. Biol. 230, 196-205 (1993).
  • K. A. Taylor & D. W. Taylor. Formation of 2-D complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar a-actinin-F-actin crosslinking. Biophys. J. 67, 1976-1983 (1994).
  • H. P. Erickson, D. W. Taylor, K. A. Taylor , and D. Bramhill. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings; structural homologs of tubulin polymers. Proc. Nat. Acad. Sci. USA. 93, 519-523 (1996).
  • X. Zhang, J. Spence, W. Qian, D. W. Taylor , and K. Taylor. Fresnel interference in point-projection imaging of purple membrane. Proc. Microscopy and Microanalysis 1995, G. W. Bailey, M. H. Ellisman, R. A. Hennigar and N. J. Zaluzec, eds. Jones and Begell Pub., New York. pp 846-847.
  • Kenneth A. Taylor and D. W. Taylor. Structural Studies of Cytoskeletal Protein Arrays Formed on Lipid Monolayers. J. Struct. Biol. 128, 75-81 (1999).
  • Thomas Wendt, D. W. Taylor, Kathy Trybus, Terri Messier, and Kenneth A. Taylor. Visualization of head-head interactions in the inhibited state of smooth muscle myosin. J. Cell Biol. 147, 1385-1390 (1999).
  • Kenneth A. Taylor, Dianne W. Taylor and Fred Schachat. α-Actinin isoforms from cardiac, smooth and skeletal muscle form polar arrays of actin filaments. J. Cell Biol. 139, 695-707 (2000).
  • Thomas Wendt, Dianne Taylor, Kathleen M. Trybus, and Kenneth Taylor. 3-D image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc. Natl. Acad. Sci. 98(8), 4361-4366 (2001).
  • Tang Jinghua, Taylor, Dianne W Taylor and Taylor, Kenneth A. The 3-D structure of α-actinin obtained by cryoelectron microscopy suggests a model for Ca2+ dependent actin binding. J. Mol. Biol. 310(4), 845-858 (2001).
  • Jun Liu, Thomas Wendt, Dianne W. Taylor and Kenneth A. Taylor. Refined model of the 10S conformation of smooth muscle myosin by cryoEM 3-D image reconstruction. J. Mol. Biol. 329(5), 963-972 (2003).
  • Liu, J., D.W. Taylor, and K.A. Taylor, A 3-D reconstruction of smooth muscle α-actinin by cryoEM reveals two different conformations at the actin binding region. J. Mol. Biol. 338(1), 115-125 (2004).
  • A. M. Makhov, D. W. Taylor, and J. D.Griffith. Two-dimensional crystallization of herpes simplex virus type 1 single-stranded DNA-binding protein, ICP8, on a lipid monolayer. Biochim. Biophys. Acta 1701, 101-108 (2004) http://dx.doi.org/10.1016/j.bbapap.2004.06.006.
  • Jun Liu, Dianne W. Taylor, Elena Krementsova, Kathy Trybus & Kenneth A. Taylor. 3-D structure of the myosin V inhibited state by cryoelectron tomography. Nature 442, 208-211 (2006).
  • Deborah F. Kelly, Dianne W. Taylor, Constantina Bakolitsa, Andrey A. Bobkov, Laurie Bankston, Robert C. Liddington and Kenneth A Taylor. Structure of the α-actinin-vinculin head domain complex determined by cryo-electron microscopy J. Mol. Biol., 357(2), 562-573 (2006).
  • Cheri M Hampton, Dianne W Taylor, Kenneth A Taylor. Novel structures for α-actinin: F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton. J. Mol. Biol. 368, 92-104 (2007) http://dx.doi.org/10.1016/j.jmb.2007.01.071.
  • Dianne W. Taylor, Deborah F. Kelly, Anchi Cheng and Kenneth A Taylor. On the freezing of lipid monolayer specimens for cryoelectron microscopy. J. Struct. Biol. 160(3), 305-312 (2007) http://dx.doi.org/10.1016/j.jsb.2007.04.011.
  • Cheri M. Hampton, Jun Liu, Dianne W. Taylor, David J. DeRosier and Kenneth A. Taylor. The 3D structure of villin as a unique F-actin cross-linker.Structure, 16(12), 1882-1891 (2008).
  • Feng Ye, Guiqing Hu, Dianne Taylor, Boris Ratnikov, Mark A. McLean, Stephen G. Sligar, Kenneth A. Taylor, and Mark H. Ginsberg. Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 188(1), 157-173 (2010). PMCID: PMC2812850.
  • Bruce A. J. Baumann, Dianne W. Taylor, Florence Tama, Patty Fagnant, Kathy Trybus & Kenneth A. Taylor. Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation. J. Mol. Biol. 415(2), 274–287 (2012). PMID: 22079364 [PubMed – in process]
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