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Evidence that C-terminal non-kinase domain of Pbs2p has a role in high osmolarity-induced nuclear localization of Hog1p.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Evidence that C-terminal non-kinase domain of Pbs2p has a role in high osmolarity-induced nuclear localization of Hog1p.
 
Creator Sharma, Pratima
Mondal, Alok K
 
Subject QD Chemistry
 
Description Mitogen-activated protein kinase (MAPK) cascade is a ubiquitous signaling module that transmits extracellular stimuli through the cytoplasm to the nucleus. In baker's yeast external high osmolarity activates high osmolarity glycerol (HOG) MAPK pathway which consists of two upstream branches (SHO1 and SLN1) and common downstream elements Pbs2p MAPKK and Hog1p MAPK. Activation of this pathway causes rapid nuclear accumulation of Hog1p, essentially leading to the expression of target genes. Previously we have isolated a PBS2 homologue (DPBS2) from osmo-tolerant and salt-tolerant yeast Debaryomyces hansenii that partially complemented pbs2 mutation in Saccharomyces cerevisiae. Here we show that by replacing C-terminal region of Dpbs2p with the homologous region of Pbs2p we could abrogate partial complementation exhibited by Dpbs2p and this was achieved due to increase in nuclear translocation of Hog1p. Thus, our result showed that in HOG pathway, MAPKK has important role in nuclear translocation of Hog1p.
 
Publisher Elsevier Science
 
Date 2005-03-25
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/189/1/alok2005.pdf
Sharma, Pratima and Mondal, Alok K (2005) Evidence that C-terminal non-kinase domain of Pbs2p has a role in high osmolarity-induced nuclear localization of Hog1p. Biochemical and biophysical research communications, 328 (4). pp. 906-13. ISSN 0006-291X
 
Relation http://www.sciencedirect.com/science/article/pii/S0006291X05000574
http://crdd.osdd.net/open/189/