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Characterization of two related drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubdes

Academic Article
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Overview

authors

  • Oegema, K.
  • Wiese, C.
  • Martin, O. C.
  • Milligan, Ronald
  • Iwamatsu, A.
  • Mitchison, T. J.
  • Zheng, Y. X.

publication date

  • February 1999

journal

  • Journal of Cell Biology  Journal

abstract

  • gamma-tubulin exists in two related complexes in Drosophila embryo extracts (Moritz, M., Y. Zheng, B.M. Alberts, and K. Oegema. 1998. J. Cell Biol. 142:1- 12). Here, we report the purification and characterization of both complexes that we name gamma-tubulin small complex (gammaTuSC; approximately 280,000 D) and Drosophila gammaTuRC ( approximately 2,200,000 D). In addition to gamma-tubulin, the gammaTuSC contains Dgrip84 and Dgrip91, two proteins homologous to the Spc97/98p protein family. The gammaTuSC is a structural subunit of the gammaTuRC, a larger complex containing about six additional polypeptides. Like the gammaTuRC isolated from Xenopus egg extracts (Zheng, Y., M.L. Wong, B. Alberts, and T. Mitchison. 1995. Nature. 378:578-583), the Drosophila gammaTuRC can nucleate microtubules in vitro and has an open ring structure with a diameter of 25 nm. Cryo-electron microscopy reveals a modular structure with approximately 13 radially arranged structural repeats. The gammaTuSC also nucleates microtubules, but much less efficiently than the gammaTuRC, suggesting that assembly into a larger complex enhances nucleating activity. Analysis of the nucleotide content of the gammaTuSC reveals that gamma-tubulin binds preferentially to GDP over GTP, rendering gamma-tubulin an unusual member of the tubulin superfamily.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cryoelectron Microscopy
  • Drosophila
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • Insect Proteins
  • Macromolecular Substances
  • Microtubules
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Binding
  • Tubulin
  • Xenopus
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Research

keywords

  • GDP
  • GTP
  • centrosome
  • cytoskeleton
  • nucleation
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.144.4.721

PubMed ID

  • 10037793
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Additional Document Info

start page

  • 721

end page

  • 733

volume

  • 144

issue

  • 4

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