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. 2003 Jun 23;161(6):1035–1040. doi: 10.1083/jcb.200301099

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Copyright © 2003, The Rockefeller University Press

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Figure 3. — Plant histidine kinase Cre1 responds to changes in turgor pressure. (A) The active (zeatin-bound) Cre1 histidine kinase is inhibited by high osmolarity stress. The double mutant sln1Δ ste11Δ GAL1-PTP2 (strain BVRY179) expressing plasmid encoding for SLN1 (sln1Δ SLN1), CRE1 (sln1Δ ADH1-CRE1 or sln1Δ CYC1-CRE1), or empty vector (sln1Δ vec), was grown in glucose media (see Materials and methods for the experimental details) in the presence (+zea) or absence (−zea) of zeatin. The activity of Hog1 was then determined in these strains before and after (0.4 M NaCl, 5 min) high osmolarity stress. (B) The time course of Hog1 activation by NaCl or sorbitol in cells expressing Cre1. The Hog1 activity was analyzed in the sln1Δ ste11Δ GAL1-PTP2 strain (BVRY179) carrying a plasmid encoding SLN1 or CRE1 or vector alone (vec). These strains were grown in glucose media (as in A) supplemented with 10 μM zeatin and stressed by 0.4 M NaCl or by 1.0 M sorbitol for indicated times. (C) Cre1 activity responds to reduction in turgor pressure. The sln1Δ ste11Δ GAL1-PTP2 strain (BVRY179) expressing SLN1 or CRE1 was incubated with sorbitol (sorb; 1.0 M, 5 min), nystatin (NYS; 10 μM, 5 min), or zymolyase (zymo; as in Fig. 2 F) before the samples were assayed for Hog1 phosphorylation. HeLa cells were treated with 1 M sorbitol for 15 min before cell extracts were prepared to determine p38 MAPK activation by immunoblot analysis using an anti-phospho-p38 antibody.