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J. Biol. Chem., Vol. 276, Issue 25, 22819-22825, June 22, 2001
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From the Yin Yang 1 (YY1) is a multifunctional
transcription factor that acts as an activator, repressor, or initiator
of transcription of numerous cellular and viral genes. Previous studies
in tissue culture model systems suggest YY1 plays a role in development and differentiation in multiple cell types, but the biological role of
YY1 in vertebrate oocytes and embryos is not well understood. Here we
analyzed expression, activity, and subcellular localization profiles of
YY1 during Xenopus laevis development. Abundant levels of
YY1 mRNA and protein were detected in early stage oocytes and in
all subsequent stages of oocyte and embryonic development through to
swimming larval stages. The DNA binding activity of YY1 was detected
only in early oocytes (stages I and II) and in embryos after the
midblastula transition (MBT), which suggested that its potential to
modulate gene expression may be specifically repressed in the
intervening period of development. Experiments to determine transcriptional activity showed that addition of YY1 recognition sites
upstream of the thymidine kinase promoter had no stimulatory or
repressive effect on basal transcription in oocytes and post-MBT embryos. Although the apparent transcriptional inactivity of YY1 in
oocytes could be explained by the absence of DNA binding activity at
this stage of development, the lack of transcriptional activity in
post-MBT embryos was not expected given the ability of YY1 to bind its
recognition elements. Subsequent Western blot and immunocytochemical analyses showed that YY1 is localized in the cytoplasm in oocytes and in cells of developing embryos well past the
MBT. These findings suggest a novel mode of YY1 regulation during early
development in which the potential transcriptional function of the
maternally expressed factor is repressed by cytoplasmic localization.
Expression, Activity, and Subcellular Localization of
the Yin Yang 1 Transcription Factor in Xenopus Oocytes and
Embryos*
,,,¶
Department of Anatomy and Cell Biology,
College of Medicine, University of Saskatchewan, Saskatoon,
Saskatchewan S7N 5E5, Canada and the § Department of
Biological Science, Florida State University, Tallahassee,
Florida 32306-3050
*
This work was supported by a Natural Sciences and
Engineering Research Council operating grant (to N. O.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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