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Vol. 14, Issue 3, 871-888, March 2003
Department of Pharmacology, University of Medicine and
Dentistry of New Jersey, Robert Wood Johnson Medical School,
Piscataway, New Jersey 08854
The NUDF protein of the filamentous fungus Aspergillus
nidulans functions in the cytoplasmic dynein pathway. It binds
several proteins, including the NUDE protein. Green fluorescent
protein-tagged NUDF and NUDA (dynein heavy chain) localize to
linearly moving dashes ("comets") that coincide with microtubule
ends. Herein, deletion of the nudE gene did not
eliminate the comets of NUDF and NUDA, but affected the behavior of
NUDA. Comets were also observed with the green fluorescent
protein-tagged NUDE and its nonfunctional C-terminal domain. In
addition, overexpressed NUDA and NUDE accumulated in specks that were
either immobile or bounced randomly. Neither comets nor specks were
observed with the functional N-terminal domain of NUDE, indicating that
these structures are not essential for NUDE function. Furthermore, NUDF
overproduction totally suppressed deletion of the nudE
gene. This implies that the function of NUDE is secondary to that of
NUDF. Unexpectedly, NUDF overproduction inhibited one conditional
nudA mutant and all tested apsA mutants.
An allele-specific interaction between the nudF and
nudA genes is consistent with a direct interaction between NUDF and dynein heavy chain. Because APSA and its yeast homolog
Num1p are cortical proteins, an interaction between the nudF and apsA genes suggests a role for
NUDF at the cell cortex.
Online version of this article contains video material for some
figures. Online version available at www.molbiolcell.org.
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