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γ-tubulin is a component of the spindle pole body that is essential for microtubule function in Aspergillus nidulans

  • Berl R. Oakley(corresponding author)
    ,
  • C. Elizabeth Oakley
    ,
  • Yisang Yoon
    ,
  • M. Katherine Jung
*Corresponding author for this work
  • Ohio State University
Scholary Output:
Contribution to journal
Article
Peer-review

Abstract

We have recently discovered that the mipA gene of A. nidulans encodes γ-tubulin, a new member of the tubulin superfamily. To determine the function of γ-tubulin in vivo, we have created a mutation in the mipA gene by integrative transformation, maintained the mutation in a heterokaryon, and determined the phenotype of the mutation in spores produced by the heterokaryon. The mutation is lethal and recessive. It strongly inhibits nuclear division, less strongly inhibits nuclear migration, and, as judged by immunofluorescence microscopy, causes a reduction in the number and length of cytoplasmic microtubules and virtually a complete absence of mitotic apparatus. We conclude that γ-tubulin is essential for microtubule function in general and nuclear division in particular. Immunofluorescence microscopy of wild-type hyphae with affinity-purified, γ-tubulin-specific antibodies reveals that γ-tubulin is a component of interphase and mitotic spindle pole bodies. We propose that γ-tubulin attaches microtubules to the spindle pole body, nucleates microtubule assembly, and establishes microtubule polarity in vivo.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 1289-1301 (13 pages)

Journal (Volume, Issue Number)

Cell (Volume 61, Issue 7)

Publication milestones

  • Published - 06/29/1990

Publication status

Published - 06/29/1990

ISSN

0092-8674

Publication IDs

  • Scopus: 0025358911
  • PubMed: 2194669
  • ORCID: /0000-0002-1618-5439/work/71658401

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Funding Details

We would like to thank Robert Day, Dr. Patrick Dunne, and Dr. John Doonan for helping develop anti-tubulin immunofluorescence procedures; Jean McGowan for assistance in setting up cultures; Yixian Zheng for initial immunofluorescence observations of Hl; and the Ohio State University College of Biological Sciences antibody facility for assistance in production of the antibodies. This work was supported by grant GM31837 from the National Institutes of Health.
FundersFunding number
NIH
-
NIGMS
R01GM031837