Please use this identifier to cite or link to this item:
|Title:||The STT3a subunit isoform of the arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress.|
|Authors:||Koiwa, Ray A.; Hasegawa, Paul M.; Mendoza, Imelda ; Pardo, José M.|
|Publisher:||American Society of Plant Biologists|
|Citation:||Plant Cell 15 (10): 2273-2284 (2003).|
|Abstract:||Arabidopsis stt3a-1 and stt3a-2 mutations cause NaCl/osmotic sensitivity that is characterized by reduced cell division in the root meristem. Sequence comparison of the STT3a gene identified a yeast ortholog, STT3, which encodes an essential subunit of the oligosaccharyltransferase complex that is involved in protein N-glycosylation. NaCl induces the unfolded protein response in the endoplasmic reticulum (ER) and cell cycle arrest in root tip cells of stt3a seedlings, as determined by expression profiling of ER stress–responsive chaperone (BiP-GUS) and cell division (CycB1;1-GUS) genes, respectively. Together, these results indicate that plant salt stress adaptation involves ER stress signal regulation of cell cycle progression. Interestingly, a mutation (stt3b-1) in another Arabidopsis STT3 isogene (STT3b) does not cause NaCl sensitivity. However, the stt3a-1 stt3b-1 double mutation is gametophytic lethal. Apparently, STT3a and STT3b have overlapping and essential functions in plant growth and developmental processes, but the pivotal and specific protein glycosylation that is a necessary for recovery from the unfolded protein response and for cell cycle progression during salt/osmotic stress recovery is associated uniquely with the function of the STT3a isoform.|
|Publisher version (URL):||DOI: 10.1105/tpc.013862|
|Appears in Collections:||(IRNAS) Artículos|
Files in This Item:
There are no files associated with this item.
Show full item record
WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.