TY - JOUR
T1 - Candidate osmosensors from Candida utilis and Kluyveromyces lactis: structural and functional homology to the Sho1p putative osmosensor from saccharomyces cerevisiae
AU - Siderius, M.H.
AU - Kolen, K.
AU - van Heerikhuizen, H.
AU - Mager, W.H.
PY - 2000
Y1 - 2000
N2 - In Saccharomyces cerevisiae, increases in external osmolarity evoke osmostress-induced signalling via the HOG MAP kinase pathway. One of the upstream components of this signal transduction route is the putative osmosensor, Sho1p. With the aim to elucidate the molecular basis of osmosensing in budding yeast, we have cloned SHO1 homologues from Candida utilis and Kluyveromyces lactis which allowed determination of conserved domains of Sho1p. Results obtained from sequence comparisons, confirmed the importance of the transmembrane domains and the SH3 domain for Sho1p function. The K. lactis and S. cerevisiae Sho1p show the highest degree of homology, the isoform from C. utilis is a shorter protein. SHO1 from C. utilis, however, did complement the osmosensitivity of the sho1ssk2ssk22 strain by restoring HOG pathway function, since Hog1p dual phosphorylation after high osmotic challenge was restored in this strain after transformation with a plasmid bearing this SHO1 homologue. (C) 2000 Elsevier Science B.V.
AB - In Saccharomyces cerevisiae, increases in external osmolarity evoke osmostress-induced signalling via the HOG MAP kinase pathway. One of the upstream components of this signal transduction route is the putative osmosensor, Sho1p. With the aim to elucidate the molecular basis of osmosensing in budding yeast, we have cloned SHO1 homologues from Candida utilis and Kluyveromyces lactis which allowed determination of conserved domains of Sho1p. Results obtained from sequence comparisons, confirmed the importance of the transmembrane domains and the SH3 domain for Sho1p function. The K. lactis and S. cerevisiae Sho1p show the highest degree of homology, the isoform from C. utilis is a shorter protein. SHO1 from C. utilis, however, did complement the osmosensitivity of the sho1ssk2ssk22 strain by restoring HOG pathway function, since Hog1p dual phosphorylation after high osmotic challenge was restored in this strain after transformation with a plasmid bearing this SHO1 homologue. (C) 2000 Elsevier Science B.V.
U2 - 10.1016/S0167-4781(00)00231-1
DO - 10.1016/S0167-4781(00)00231-1
M3 - Article
SN - 0167-4781
VL - 1517
SP - 143
EP - 147
JO - Biochimica et Biophysica Acta. Gene Structure and Expression
JF - Biochimica et Biophysica Acta. Gene Structure and Expression
ER -