Analysis of Coiled-Coil Interactions between Core Proteins of the Spindle Pole Body

Zizlsperger, Nora; Malashkevich, V.N.; Pillay, Shirin; Keating, Amy E.

doi:10.1021/bi801378z

Cited by 20 publications

(38 citation statements)

References 60 publications

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“…A stunning finding from this work is that the central plaque is organized around a paracrystalline array of the Spc42 protein (Bullitt et al 1997). This protein is nearly all coiled coil for which there is a crystal structure (Zizlsperger et al 2008), and it packs in a hexagonal array as seen in cryo-EM of isolated SPBs (Bullitt et al 1997). This structural feature of the SPB was also observed in situ using electron tomography (Geiser et al 1993;Kilmartin et al 1993;O'Toole et al 1999).…”

Section: The Parts Listmentioning

confidence: 71%

Mitotic Spindle Form and Function

2012

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The Saccharomyces cerevisiae mitotic spindle in budding yeast is exemplified by its simplicity and elegance. Microtubules are nucleated from a crystalline array of proteins organized in the nuclear envelope, known as the spindle pole body in yeast (analogous to the centrosome in larger eukaryotes). The spindle has two classes of nuclear microtubules: kinetochore microtubules and interpolar microtubules. One kinetochore microtubule attaches to a single centromere on each chromosome, while approximately four interpolar microtubules emanate from each pole and interdigitate with interpolar microtubules from the opposite spindle to provide stability to the bipolar spindle. On the cytoplasmic face, two to three microtubules extend from the spindle pole toward the cell cortex. Processes requiring microtubule function are limited to spindles in mitosis and to spindle orientation and nuclear positioning in the cytoplasm. Microtubule function is regulated in large part via products of the 6 kinesin gene family and the 1 cytoplasmic dynein gene. A single bipolar kinesin (Cin8, class Kin-5), together with a depolymerase (Kip3, class Kin-8) or minus-end-directed kinesin (Kar3, class Kin-14), can support spindle function and cell viability. The remarkable feature of yeast cells is that they can survive with microtubules and genes for just two motor proteins, thus providing an unparalleled system to dissect microtubule and motor function within the spindle machine.

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Section: The Parts Listmentioning

confidence: 71%

Mitotic Spindle Form and Function

2012

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“…It is particularly interesting that all three proteins, Scy, DivIVA, and FilP, are coiled-coil proteins with highly similar domain organization: a short coiled-coil domain, followed by a linker and a second coiled-coil domain (22). In addition to other bacterial examples of coiled-coil polarity determinants, such as TipN or PopZ of C. crescentus (28)(29)(30)(31)(32), the spindle pole body, specialized for centromere function in yeast, is also dominated by long coiledcoil proteins (33,34), suggesting further structural similarities between organizing centers in bacteria and eukaryotes.…”

Section: Discussionmentioning

confidence: 99%

Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth inStreptomyces

Holmes¹,

Walshaw

Leggett³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

146

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Polarized growth in eukaryotes requires polar multiprotein complexes. Here, we establish that selection and maintenance of cell polarity for growth also requires a dedicated multiprotein assembly in the filamentous bacterium, Streptomyces coelicolor. We present evidence for a tip organizing center and confirm two of its main components: Scy (Streptomyces cytoskeletal element), a unique bacterial coiled-coil protein with an unusual repeat periodicity, and the known polarity determinant DivIVA. We also establish a link between the tip organizing center and the filamentforming protein FilP. Interestingly, both deletion and overproduction of Scy generated multiple polarity centers, suggesting a mechanism wherein Scy can both promote and limit the number of emerging polarity centers via the organization of the Scy-DivIVA assemblies. We propose that Scy is a molecular "assembler," which, by sequestering DivIVA, promotes the establishment of new polarity centers for de novo tip formation during branching, as well as supporting polarized growth at existing hyphal tips.bacterial polarized growth | polar multiprotein assembly | cell division | modified hendecad coiled coil H ow organisms, cells, or tissues establish polarity is one of the fundamental questions in developmental biology. In eukaryotes, from unicellular organisms to multicellular plants and animals, some of the core mechanisms for generating polarity are conserved (1). Sites for polarization must be selected using positional markers, followed by the recruitment of a complex assembly, which, in turn, orients cytoskeletal filaments that deliver vesicles to the particular sites. A specific example of polarity is polarized growth, during which cells select a single polarization site and generate elongated, cylindrical shapes, such as neuronal dendrites in animals, root hairs and pollen tubes in plants, hyphal growth of filamentous fungi, elongation of Schizosaccharomyces pombe, or the short period of polarized growth during budding in Saccharomyces cerevisiae. However, the presumed earliest examples of polarized growth can be found in bacteria. These include the actinomycete Streptomyces coelicolor, which is used as a model organism for studying morphological differentiation and filamentous growth.The complex life cycle of S. coelicolor begins with an ovoid spore that contains a single chromosome. During germination, long, multigenomic filaments (germ tubes) are formed, which branch regularly to generate a network of hyphal filaments. Branching is a necessity for exponential growth because the rate of tip elongation cannot exceed a certain maximum; hence, there is an exponential increase in the number of new tips. New tips develop on the lateral wall well behind the existing tip, a phenomenon also observed and described as apical dominance in eukaryotic filamentous fungi. When grown on semisolid agar medium, these hyphal filaments first grow across and into the solid medium, generating the vegetative mycelium, followed by the formation of an aerial mycelium by h...

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“…[15] Im Polkörperchen des mitotischen Spindelapparats in Hefezellen wird der Abstand zwischen den Plaques durch die Länge eines parallelen Homodimers innerhalb der Verbindungsproteine festgelegt. [6,16] Die Aminosäuresequenz der Abstandhalter unterscheidet sich zwischen den Spezies beträchtlich, wobei die Positionen a und d noch am ehesten konserviert sind. [17] Die Sequenzdivergenz ist lediglich dadurch eingeschränkt, dass die Fähigkeit zur Coiled-Coil-Bildung aufrechterhalten bleiben muss, wofür vorrangig die Positionen a und d zuständig sind.…”

Section: Strukturelle Funktionenunclassified

Selbstorganisation von Coiled‐Coils in der synthetischen Biologie: Inspiration und Fortschritt

Marsden

Kros

2010

Angewandte Chemie

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Die biologische Selbstorganisation ist ein sehr komplexer Vorgang und lässt sich im Grunde als Bottom‐up‐Synthese verstehen, die biomolekulare Bausteine von präzise festgelegter Form, Größe, Hydrophobie und Funktionalisierung zu Funktionsmaterialien zusammenfügt. Im Bereich der supramolekularen Chemie haben Wissenschaftler von den Selbstorganisationsvorgängen in der Natur gelernt, wie sich das Zusammenspiel vieler kleiner Kräfte beherrschen lässt, um zu komplexen selbstorganisierten Nanomaterialien zu gelangen. Das Coiled‐Coil‐Motiv ist ein in der Natur weit verbreiteter Baustein, der außerdem ein großes Potenzial in der synthetischen Biologie hat. In diesem Aufsatz untersuchen wir die Rolle des Coiled‐Coil‐Motivs in der natürlichen Selbstorganisation und fassen zusammen, welche Fortschritte bei der Verwendung dieses Motivs in der Synthese von funktionellen Einheiten, Aggregaten und Systemen erzielt wurden.

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Analysis of Coiled-Coil Interactions between Core Proteins of the Spindle Pole Body

Cited by 20 publications

References 60 publications

Mitotic Spindle Form and Function

Mitotic Spindle Form and Function

Coiled-coil protein Scy is a key component of a multiprotein assembly controlling polarized growth inStreptomyces

Selbstorganisation von Coiled‐Coils in der synthetischen Biologie: Inspiration und Fortschritt

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