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Molecular and Cellular Biology, December 1998, p. 7575-7583, Vol. 18, No. 12
Departments of
Biochemistry1 and
Molecular Physiology
and Biophysics,2 Vanderbilt University
School of Medicine, Nashville, Tennessee 37232-0146
Received 12 June 1998/Returned for modification 10 July
1998/Accepted 3 September 1998
The M26 meiotic recombination hot spot in the
ade6 gene of Schizosaccharomyces pombe is
activated by the heterodimeric M26 binding protein
Mts1-Mts2. The individual Mts1 (Atf1, Gad7) and Mts2 (Pcr1) proteins
are also transcription factors involved in developmental decisions. We
report that the Mts proteins are key effectors of at least two distinct
classes of developmental decisions regulated by the mitogen-activated
protein (MAP) kinase cascade. The first class (osmoregulation, spore
viability, and spore quiescence) requires the Spc1 MAP kinase and the
Mts1 protein but does not require the Mts2 protein. The second class
(mating, meiosis, and recombination hot spot activation) requires the
Spc1 kinase and the Mts1-Mts2 heterodimer. Northern and Western
blotting eliminated any significant role for the Spc1 kinase in
regulating the expression levels of the Mts proteins. Gel mobility
shift experiments indicated that the Mts1-Mts2 heterodimer does not
need to be phosphorylated to bind to ade6-M26 DNA in vitro.
However, in vivo dimethyl sulfate footprinting demonstrated that
protein-DNA interaction within cells is dependent upon the Spc1 MAP
kinase, which phosphorylates the Mts1 protein. Thus, the Spc1 kinase
helps regulate the effector activities of the Mts1-Mts2 heterodimer in
part by modulating its ability to occupy the M26 DNA site
in vivo. Meiotic recombination hot spot function is likely the result
of DNA conformational changes imparted by binding of the Mts1-Mts2
meiotic transcription factor.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Regulation of the Mts1-Mts2-Dependent
ade6-M26 Meiotic Recombination Hot Spot and Developmental
Decisions by the Spc1 Mitogen-Activated Protein Kinase of Fission
Yeast
*
Corresponding author. Mailing address: Department of
Biochemistry, Vanderbilt University School of Medicine, 621 Light Hall, Nashville, TN 37232-0146. Phone: (615) 322-3063. Fax: (615) 343-0704. E-mail: wahlswp{at}ctrvax.vanderbilt.edu.
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