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Molecular and Cellular Biology, December 1999, p. 8461-8468, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Conservation of Histone Binding and Transcriptional
Repressor Functions in a Schizosaccharomyces pombe
Tup1p Homolog
Yukio
Mukai,1,2,*
Eri
Matsuo,1
Sharon Y.
Roth,2 and
Satoshi
Harashima1
Department of Biotechnology, Graduate School
of Engineering, Osaka University, Suita, Osaka 565-0871, Japan,1 and Department of Biochemistry
and Molecular Biology, University of Texas M. D. Anderson
Cancer Center, Houston, Texas 770302
Received 24 May 1999/Returned for modification 30 June
1999/Accepted 13 September 1999
The Ssn6p-Tup1p corepressor complex is important to the regulation
of several diverse genes in Saccharomyces cerevisiae and serves as a model for corepressor functions. To investigate the evolutionary conservation of these functions, sequences homologous to
the S. cerevisiae TUP1 gene were cloned from
Kluyveromyces lactis (TUP1) and
Schizosaccharomyces pombe (tup11+).
Interestingly, while the K. lactis TUP1 gene complemented
an S. cerevisiae tup1 null mutation, the S. pombe
tup11+ gene did not, even when expressed under the
control of the S. cerevisiae TUP1 promoter. However, an
S. pombe Tup11p-LexA fusion protein repressed transcription
of a corresponding reporter gene, indicating that this Tup1p homolog
has intrinsic repressor activity. Moreover, a chimeric protein
containing the amino-terminal Ssn6p-binding domain of S. cerevisiae Tup1p and 544 amino acids from the C-terminal region
of S. pombe Tup11p complemented the S. cerevisiae
tup1 mutation. The failure of native S. pombe Tup11p
to complement loss of Tup1p functions in S. cerevisiae
corresponds to an inability to bind to S. cerevisiae Ssn6p
in vitro. Disruption of tup11+ in combination
with a disruption of tup12+, another
TUP1 homolog gene in S. pombe, causes a defect
in glucose repression of fbp1+, suggesting that
S. pombe Tup1p homologs function as repressors in S. pombe. Furthermore, Tup11p binds specifically to histones H3 and
H4 in vitro, indicating that both the repression and histone binding
functions of Tup1p-related proteins are conserved across species.
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030. Phone: (713) 792-2549. Fax: (713) 790-0329. E-mail: ymukai{at}odin.mdacc.tmc.edu.
Molecular and Cellular Biology, December 1999, p. 8461-8468, Vol. 19, No. 12
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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