Figure iii. Protein folding chaperones.
(A) The HSP90/60, SSA1, and SSA2 clusters as they appear in the genomic cluster shown in Figure1. Many of these chaperones are known to be co-regulated by the transcription factor Hsf1p in response to heat shock. Known targets of Hsf1p are shown in red (Kobayashi and McEntee, 1993, Tamai et al., 1994, Liu et al., 1999; Morano et al., 1999). Although these genes are coordinately induced in response to heat shock and diamide treatment, they are divergently expressed in response to other environmental transitions, reflecting differences in their regulation under these conditions. Adjacent genes in this display that are likely to cross-hybridize on the arrays are denotated with an astrisk.

(B) The KAR2 and LHS1 clusters as they appear in the genomic cluster shown in Figure 1. Reduction by DTT prevents proper disulfide bond formation in the ER, activating the transcription factor Hac1p as part of the Unfolded Protein Respnse (Jamsa et al., 1994). Genes known to be regulated by Hac1p are labled in purple (Travers et al. 2000, Kawahara et al., 1997; Mori et al., 1998). Similar to the cytoplasmic and mitochondrial chaperones, genes in the " KAR2 cluster" and "LHS1 cluster" are differentially expressed in response to other conditions, including heat shock and diamide treatment.