Presence of a basic secretory protein in xylem sap and shoots of poplar in winter and its physicochemical activities against winter environmental conditions
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XSP25, previously shown to be the most abundant hydrophilic protein in xylem sap of Populus nigra in winter, belongs to a secretory protein family in which the arrangement of basic and acidic amino acids is conserved between dicotyledonous and monocotyledonous species. Its gene expression was observed at the same level in roots and shoots under long-day conditions, but highly induced under short-day conditions and at low temperatures in roots, especially in endodermis and xylem parenchyma in the root hair region of Populus trichocarpa, and its protein level was high in dormant buds, but not in roots or branches. Addition of recombinant PtXSP25 protein mitigated the denaturation of lactate dehydrogenase by drying, but showed only a slight effect on that caused by freeze–thaw cycling. Recombinant PtXSP25 protein also showed ice recrystallization inhibition activity to reduce the size of ice crystals, but had no antifreezing activity. We suggest that PtXSP25 protein produced in shoots and/or in roots under short-day conditions and at non-freezing low temperatures followed by translocation via xylem sap to shoot apoplast may protect the integrity of the plasma membrane and cell wall functions from freezing and drying damage in winter environmental conditions.
KeywordsApoplast Basic secretory protein Dry Freeze Ice crystal Short day Winter Xylem sap
Bovine serum albumin
Basic secretory protein
Ice recrystallization inhibition
Non-freezing low temperature
Real-time quantitative reverse-transcription polymerase chain reaction
Sodium dodecyl sulfate
Xylem sap protein
We thank Drs. Misato Ohtani and Taku Demura of the Nara Institute of Science and Technology for their help regarding aseptic culture and genetic transformation of poplar. This work was supported in part by a Grant-in-Aid for Scientific Research (B) and for Scientific Research on Innovative Areas (24114006) to S.S.
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