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J Biol Chem, Vol. 273, Issue 37, 24131-24138, September 11, 1998
From the Department of Anatomy and Cell Biology, College of
Physicians and Surgeons, Columbia University,
New York, New York 10032
A novel component of the ubiquitination system,
called NOSA, is essential for cellular differentiation in
Dictyostelium discoideum. Disruption of nosA
does not affect the growth rate but causes an arrest in development
after the cells have aggregated. nosA contains seven exons
and codes for a developmentally regulated 3.5-kb mRNA. The 125-kDa
NOSA protein is present in the cytosol at constant levels during growth
and development. The C-terminal region of NOSA has homology with
ubiquitin fusion degradation protein-2 (UFD2) of Saccharomyces
cerevisiae and putative homologs in Caenorhabditis
elegans and humans. UFD2 is involved in the ubiquitin-mediated
degradation of model substrates in which ubiquitin forms part of the
translation product, but ufd2 mutants have no detected
phenotype. In accord with the homology to UFD2, we found differences in
the ubiquitination patterns between nosA mutants and their
parental cell line. While general in vivo and in
vitro ubiquitination is minimally affected, ubiquitination of
individual proteins is altered throughout growth and development in
nosA mutants. These findings suggest that events involving
ubiquitination are critical for progression through the aggregate stage
of the Dictyostelium life cycle.
A Novel Component Involved in Ubiquitination Is Required for
Development of Dictyostelium discoideum
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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