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stan burgess

Hiroshi Imai, Tomohiro Shima, Kazuo Sutoh, Matthew L Walker, Peter J Knight, Takahide Kon, Stan A Burgess
Cytoplasmic dynein is a dimeric AAA(+) motor protein that performs critical roles in eukaryotic cells by moving along microtubules using ATP. Here using cryo-electron microscopy we directly observe the structure of Dictyostelium discoideum dynein dimers on microtubules at near-physiological ATP concentrations. They display remarkable flexibility at a hinge close to the microtubule binding domain (the stalkhead) producing a wide range of head positions. About half the molecules have the two heads separated from one another, with both leading and trailing motors attached to the microtubule...
September 14, 2015: Nature Communications
Yusuke S Kato, Toshiki Yagi, Sarah A Harris, Shin-ya Ohki, Kei Yura, Youské Shimizu, Shinya Honda, Ritsu Kamiya, Stan A Burgess, Masaru Tanokura
Flagellar dyneins are essential microtubule motors in eukaryotes, as they drive the beating motions of cilia and flagella. Unlike myosin and kinesin motors, the track binding mechanism of dyneins and the regulation between the strong and weak binding states remain obscure. Here we report the solution structure of the microtubule-binding domain of flagellar dynein-c/DHC9 (dynein-c MTBD). The structure reveals a similar overall helix-rich fold to that of the MTBD of cytoplasmic dynein (cytoplasmic MTBD), but dynein-c MTBD has an additional flap, consisting of an antiparallel b sheet...
November 4, 2014: Structure
Neil Billington, Derek J Revill, Stan A Burgess, Peter D Chantler, Peter J Knight
We show that negative-stain electron microscopy and image processing of nucleotide-free (apo) striated muscle myosin-2 subfragment-1 (S1), possessing one light chain or both light chains, is capable of resolving significant amounts of structural detail. The overall appearance of the motor and the lever is similar in rabbit, scallop and chicken S1. Projection matching of class averages of the different S1 types to projection views of two different crystal structures of apo S1 shows that all types most commonly closely resemble the appearance of the scallop S1 structure rather than the methylated chicken S1 structure...
February 20, 2014: Journal of Molecular Biology
Anthony J Roberts, Takahide Kon, Peter J Knight, Kazuo Sutoh, Stan A Burgess
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work...
November 2013: Nature Reviews. Molecular Cell Biology
Anthony J Roberts, Bara Malkova, Matt L Walker, Hitoshi Sakakibara, Naoki Numata, Takahide Kon, Reiko Ohkura, Thomas A Edwards, Peter J Knight, Kazuo Sutoh, Kazuhiro Oiwa, Stan A Burgess
Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar dynein-c and a cytoplasmic dynein motor domain in different nucleotide states. The structures show key sites of conformational change within the AAA+ ring and a large rearrangement of the "linker" domain, involving a hinge near its middle...
October 10, 2012: Structure
Anthony J Roberts, Stan A Burgess
Despite more than 40 years of investigation since the discovery of dynein [Gibbons, I. R. and Rowe, A. J. (1965). Science149, 424-426] our understanding of how this microtubule-based motor generates force and movement remains frustratingly incomplete at the atomic level. Electron microscopy (EM) has played a major role in establishing dynein's complex architecture and its nucleotide-dependent conformational changes. In this chapter we review recent structural studies and describe in detail negative stain EM and computational single-particle image processing techniques that have been used to investigate dynein...
2009: Methods in Cell Biology
Olusola A Oke, Stan A Burgess, Eva Forgacs, Peter J Knight, Takeshi Sakamoto, James R Sellers, Howard White, John Trinick
Using electron microscopy and image processing, we have observed myosin 5a modified with lever arms of different lengths (four, six, and eight calmodulin-binding IQ domains) and orientations walking along actin filaments. Step lengths were dependent on lever length: 8IQ > 6IQ > 4IQ, which is consistent with myosin 5a having evolved to walk straight along actin. Lead heads were mostly in the prepowerstroke state, tethered there by the trail head. However, improved image processing showed that in 5-10% of molecules the lead motor was in the postpowerstroke state...
February 9, 2010: Proceedings of the National Academy of Sciences of the United States of America
Anthony J Roberts, Naoki Numata, Matt L Walker, Yusuke S Kato, Bara Malkova, Takahide Kon, Reiko Ohkura, Fumio Arisaka, Peter J Knight, Kazuo Sutoh, Stan A Burgess
Dynein ATPases power diverse microtubule-based motilities. Each dynein motor domain comprises a ring-like head containing six AAA+ modules and N- and C-terminal regions, together with a stalk that binds microtubules. How these subdomains are arranged and generate force remains poorly understood. Here, using electron microscopy and image processing of tagged and truncated Dictyostelium cytoplasmic dynein constructs, we show that the heart of the motor is a hexameric ring of AAA+ modules, with the stalk emerging opposite the primary ATPase site (AAA1)...
February 6, 2009: Cell
Takahide Kon, Kenji Imamula, Anthony J Roberts, Reiko Ohkura, Peter J Knight, I R Gibbons, Stan A Burgess, Kazuo Sutoh
Coupling between ATPase and track binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled coil stalk that must mediate communication between them, but the underlying mechanism remains unclear. Here we show that changes in registration between the two helices of the coiled coil can perform this function. We locked the coiled coil at three specific registrations using oxidation to disulfides of paired cysteine residues introduced into the two helices...
March 2009: Nature Structural & Molecular Biology
Hyun Suk Jung, Stan A Burgess, Neil Billington, Melanie Colegrave, Hitesh Patel, Joseph M Chalovich, Peter D Chantler, Peter J Knight
The myosin 2 family of molecular motors includes isoforms regulated in different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain, whereas scallop striated adductor-muscle myosin is activated by direct calcium binding to its essential light chain. The paired heads of inhibited molecules from myosins regulated by phosphorylation have an asymmetric arrangement with motor-motor interactions. It was unknown whether such interactions were a common motif for inactivation used in other forms of myosin-linked regulation...
April 22, 2008: Proceedings of the National Academy of Sciences of the United States of America
Stan A Burgess, Shuizi Yu, Matt L Walker, Rhoda J Hawkins, Joseph M Chalovich, Peter J Knight
Remodelling the contractile apparatus within smooth muscle cells allows effective contractile activity over a wide range of cell lengths. Thick filaments may be redistributed via depolymerisation into inactive myosin monomers that have been detected in vitro, in which the long tail has a folded conformation. Using negative stain electron microscopy of individual folded myosin molecules from turkey gizzard smooth muscle, we show that they are more compact than previously described, with heads and the three segments of the folded tail closely packed...
October 5, 2007: Journal of Molecular Biology
Norito Kotani, Hitoshi Sakakibara, Stan A Burgess, Hiroaki Kojima, Kazuhiro Oiwa
Inner-arm dynein-f of Chlamydomonas flagella is a heterodimeric dynein. We performed conventional in vitro motility assays showing that dynein-f translocates microtubules at the comparatively low velocity of approximately 1.2 microm/s. From the dependence of velocity upon the surface density of dynein-f, we estimate its duty ratio to be 0.6-0.7. The relation between microtubule landing rate and surface density of dynein-f are well fitted by the first-power dependence, as expected for a processive motor. At low dynein densities, progressing microtubules rotate erratically about a fixed point on the surface, at which a single dynein-f molecule is presumably located...
August 1, 2007: Biophysical Journal
Dean Clarke, Stephen Griffin, Lucy Beales, Corine St Gelais, Stan Burgess, Mark Harris, David Rowlands
The p7 protein of hepatitis C virus functions as an ion channel both in vitro and in cell-based assays and is inhibited by amantadine, long alkyl chain imino-sugar derivatives, and amiloride compounds. Future drug design will be greatly aided by information on the stoichiometry and high resolution structure of p7 ion channel complexes. Here, we have refined a bacterial expression system for p7 based on a glutathione S-transferase fusion methodology that circumvents the inherent problems of hydrophobic protein purification and the limitations of chemical synthesis...
December 1, 2006: Journal of Biological Chemistry
Stan A Burgess, Matt L Walker, Kavitha Thirumurugan, John Trinick, Peter J Knight
Flexible macromolecules pose special difficulties for structure determination by crystallography or NMR. Progress can be made by electron microscopy, but electron cryo-microscopy of unstained, hydrated specimens is limited to larger macromolecules because of the inherently low signal-to-noise ratio. For three-dimensional structure determination, the single particles must be invariant in structure. Here, we describe how we have used negative staining and single-particle image processing techniques to explore the structure and flexibility of single molecules of two motor proteins: myosin and dynein...
September 2004: Journal of Structural Biology
Stan Burgess, Matt Walker, Peter J Knight, John Sparrow, Stephan Schmitz, Gerald Offer, Belinda Bullard, Kevin Leonard, John Holt, John Trinick
Here, we report on the structure and in situ location of arthrin (monoubiquitinated actin). Labelling of insect muscle thin filaments with a ubiquitin antibody reveals that every seventh subunit along the filament long-pitch helices is ubiquitinated. A three-dimensional reconstruction of frozen-hydrated arthrin filaments was produced. This was based on a novel algorithm that divides filament images into short segments that are used for single-particle image processing. Difference maps with an actin filament reconstruction locate ubiquitin at the side of actin sub-domain 1 opposite where myosin binds...
August 27, 2004: Journal of Molecular Biology
Stan A Burgess, Peter J Knight
Dyneins are the largest and most complex of the three classes of linear motor proteins in eukaryotic cells. The mass of the dynein motor domain is about ten times that of the other microtubule motor, kinesin. Dynein's homology with the AAA+ superfamily of mechanoenzymes distinguishes it from both kinesin and myosin, which share a common fold and ancestry as members of the G-protein superfamily. In contrast to the other motor proteins, little is known about the mechanism of dynein; its three-dimensional structure is unknown even at low resolution...
April 2004: Current Opinion in Structural Biology
Stan A Burgess, Matt L Walker, Hitoshi Sakakibara, Peter J Knight, Kazuhiro Oiwa
Dynein ATPases are microtubule motors that are critical to diverse processes such as vesicle transport and the beating of sperm tails; however, their mechanism of force generation is unknown. Each dynein comprises a head, from which a stalk and a stem emerge. Here we use electron microscopy and image processing to reveal new structural details of dynein c, an isoform from Chlamydomonas reinhardtii flagella, at the start and end of its power stroke. Both stem and stalk are flexible, and the stem connects to the head by means of a linker approximately 10 nm long that we propose lies across the head...
February 13, 2003: Nature
Stan Burgess, Matt Walker, Fei Wang, James R Sellers, Howard D White, Peter J Knight, John Trinick
We have used electron microscopy and single-particle image processing to study head conformation in myosin V molecules. We find that in the presence of ATP, many heads have a sharply angled conformation that is rare in its absence. The sharply angled conformation is similar to a myosin II atomic structure proposed to mimic the prepower stroke state. The leading head in molecules attached to actin by both heads has a similar conformation, but is also sharply angled in a second plane by tethering through the trail head...
December 23, 2002: Journal of Cell Biology
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