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Vol. 12, Issue 2, 407-419, February 2001
¶ and
The Schizosaccharomyces pombe stress-activated
Sty1p/Spc1p mitogen-activated protein (MAP) kinase regulates gene
expression through the Atf1p and Pap1p transcription factors, homologs
of human ATF2 and c-Jun, respectively. Mcs4p, a response
regulator protein, acts upstream of Sty1p by binding the Wak1p/Wis4p
MAP kinase kinase kinase. We show that phosphorylation of Mcs4p on a
conserved aspartic acid residue is required for activation of Sty1p
only in response to peroxide stress. Mcs4p acts in a conserved phospho-relay system initiated by two PAS/PAC domain-containing histidine kinases, Mak2p and Mak3p. In the absence of Mak2p or Mak3p,
Sty1p fails to phosphorylate the Atf1p transcription factor or induce
Atf1p-dependent gene expression. As a consequence, cells lacking Mak2p
and Mak3p are sensitive to peroxide attack in the absence of Prr1p, a
distinct response regulator protein that functions in association with
Pap1p. The Mak1p histidine kinase, which also contains PAS/PAC repeats,
does not regulate Sty1p or Atf1p but is partially required for Pap1p-
and Prr1p-dependent transcription. We conclude that the transcriptional
response to free radical attack is initiated by at least two distinct
phospho-relay pathways in fission yeast.
Division of Yeast Genetics and §Protein
Structure, National Institute for Medical Research, The Ridgeway, Mill
Hill, London, NW7 1AA United Kingdom; and School of
Biochemistry and Genetics, University of Newcastle-upon-Tyne, Tyne and
Wear, NE2 4HH United Kingdom
Permanent address: Department of Molecular
Microbiology, Research Institute for Microbial Diseases, Osaka
University, 3-1 Yamadaoka Suita, Osaka 565, Japan.
¶
Corresponding authors. E-mail addresses:
jmillar{at}nimr.mrc.ac.uk and B.A.Morgan{at}newcastle.ac.uk.
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