Using antibodies raised against two sunflower small heat shock proteins (sHSPs), we have detected immunologically related proteins in unstressed vegetative tissues from the resurrection plant Craterostigma plantagineum. In whole plants, further accumulation of these polypeptides was induced by heat-shock or water-stress. In desiccation-intolerant Craterostigma callus tissue, we failed to detect sHSP-related polypeptides, but their expression, and the concurrent acquisition of desiccation tolerance was induced by exogenous abscisic acid (ABA) treatment. In untressed plants, the cross-reacting polypeptides were abundant in the roots and lower part of the shoots, where they showed homogeneous tissue-distributions. This constitutive expression is novel for vegetative tissues of higher plants, and resembles the expression patterns of sHSPs in desiccation-tolerant zygotic embryos and germinating seeds.Angiosperms only tolerate severe protoplasmic dehydration during the late stages of zygotic embryogenesis in seed development. In some cases, the desiccation tolerance of the mature embryo is preserved during the early stages of germination. Later in development, the vegetative tissues of most plants become desiccation-intolerant. Exceptions to this comprise different species, which include mosses (i.e., Tortula ruralis), pteridophytes (Polypodium virginianum, Selaginella lepidophyla, etc.), and even a few higher plants termed resurrection plants [7, and references therein]. Among the latter, Craterostigma plantagineum (Scrophulariaceae) has been used as model system for molecular analyses of desiccation tolerance. Most studies of Craterostigma have focused on the characterization of genes induced by dehydration [21, 22]. Many of these genes show sequence homologies with genes abundantly expressed in desiccation-tolerant zygotic embryos [reviewed in 3, 4].In the course of our studies on gene expression during late embryogenesis in sunflower, we isolated and characterized cDNAs encoding two seed-stored sHSPs, Ha HSP17.6 and Ha HSP17.9 [2,11]. Their predicted amino acid se-