Involvement of the compatible solutes trehalose and sucrose in the response to salt stress of a cyanobacterial Scytonema species isolated from desert soils.
The response to moderate salt stress of a Scytonema species isolated from a soil crust in the arid region of central Australia was studied. An increase in intracellular trehalose and sucrose concentrations was detected by NMR and HPLC analysis following salt stress, maximal amounts being produced by exposure to 150 mM NaCl after 48 h. When the organism was subsequently returned to normal growth conditions, the cellular concentrations of these solutes decreased. The biosynthesis of trehalose and sucrose was studied and found, in both cases, to involve both sugar phosphate synthase and phosphatase enzymes. The combined synthase activities and the individual phosphatase activities in cell extracts were increased by salt stress. Trehalose phosphorylase was the only catabolic enzyme detected for trehalose; neither trehalase nor phosphotrehalase activities could be detected. This is the first report of trehalose phosphorylase activity in cyanobacteria. Both trehalose and sucrose phosphorylase activities increased in salt-stressed cells, whereas the activity of invertase did not change.
Page-Sharp
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Division of Biochemistry and Molecular Biology, Faculty of Science, The Australian National University, Canberra, ACT, Australia.
Behm
C A
CA
Smith
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GD
D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000378:metabolism*; D005964:Glucosyltransferases / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D012492:Salts; D012988:Soil Microbiology; D013395:Sucrose / Q000032:analysis; D014199:Trehalose / Q000032:analysis
D012492:Salts; D013395:Sucrose; D014199:Trehalose; D005964:Glucosyltransferases; C023181:alpha,alpha-trehalose phosphorylase; C025901:sucrose phosphorylase