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From the Control over the nuclear transport of transcription factors
(TFs) represents a level of gene regulation integral to cellular
processes such as differentiation, transformation and signal
transduction. The Saccharomyces cerevisiae TF SWI5 is excluded
from the nucleus in a cell cycle-dependent fashion, mediated by
phosphorylation by the cyclin-dependent kinase (cdk) CDC28. Nuclear
entry occurs in G
Volume 270,
Number 29,
Issue of July 21, pp. 17064-17067, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
. 
-galactosidase fusion proteins
carrying SWI5 amino acids 633-682, including the nuclear
localization sequence (NLS:
Lys-Lys-Tyr-Glu-Asn-ValVal-Ile-Lys-Arg-Ser-Pro-Arg-Lys-Arg-Gly-Arg-ProArg-Lys)
were analyzed for subcellular localization in appropriate
temperature-sensitive yeast strains blocked in G
or
G
/M using indirect immunofluorescence, and for nuclear
import kinetics in living rat hepatoma or Vero African green monkey
kidney cells microinjected with fluorescently labeled bacterially
expressed protein and quantitative confocal laser microscopy. Cell
cycle-dependent nuclear localization in yeast was both NLS and cdk
site-dependent, whereby mutation of the cdk site serines (Ser and Ser
) to alanine resulted in constitutive
nuclear localization. In mammalian cells, the SWI5 fusion proteins were
similarly transported to the nucleus in an NLS-dependent fashion, while
the mutation to Ala of the cdk site serines increased the maximal level
of nuclear accumulation from about 1- to over 8-fold. We suggest that
phosphorylation at the cdk sites inhibits nuclear transport of SWI5,
consistent with our previous observations for the inhibition of SV40
large tumor antigen nuclear transport by phosphorylation by the cdk
cdc2. The results indicate for the first time that a yeast NLS and,
fascinatingly, its regulatory mechanisms are functional in higher
eukaryotes, implying the universal nature of regulatory signals for
protein transport to the nucleus.
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