Cold acclimation enhances the activity of plasma membrane Ca2+ ATPase in winter rye leaves. Puhakainen, T., Pihakaski-Maunsbach, K., Widell, S., & Sommarin, M. Plant Physiology and Biochemistry, 37(3):231–239, March, 1999. ![Cold acclimation enhances the activity of plasma membrane Ca2+ ATPase in winter rye leaves [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Exposure of plant cells and tissues to low or freezing temperatures often lead to uncontrolled and detrimental ion leakage. Therefore, when plants acclimate to low temperatures, processes that control ionic homeostasis are important. Here we characterized H+ ATPase and ATP-dependent Ca2+ transport activities in isolated plasma membranes of cold-acclimated and non-acclimated winter rye leaves (Secale cereale L. cv. Voima). Cold acclimation resulted in a two-fold higher Ca2+ transport activity, significantly different (P = 0.021) from that of non-acclimated rye, whereas only a small increase in H+ ATPase activity, measured as ATP hydrolysis, was observed in cold-acclimated compared to non-acclimated preparations. In plasma membranes, extensively washed with EDTA and Brij 58 to remove endogenous calmodulin, Ca2+ transport activity increased to about double by calmodulin addition, with both non-acclimated and cold-acclimated material. Uptake of Ca2+ was seen within the pHrange analyzed (pH 6–8), with an optimum at pH 7.2 with both materials, and both in the absence and in the presence of calmodulin. The increase in activity of ATP-dependent Ca2+ transport in cold-acclimated rye plasma membranes probably reflects the capacity needed to sustain the resting level of cytosolic Ca2+ concentration that is characteristic to the cold-acclimated situation.
@article{puhakainen_cold_1999,
title = {Cold acclimation enhances the activity of plasma membrane {Ca2}+ {ATPase} in winter rye leaves},
volume = {37},
issn = {0981-9428},
url = {https://www.sciencedirect.com/science/article/pii/S0981942899800382},
doi = {10/dcxvrr},
abstract = {Exposure of plant cells and tissues to low or freezing temperatures often lead to uncontrolled and detrimental ion leakage. Therefore, when plants acclimate to low temperatures, processes that control ionic homeostasis are important. Here we characterized H+ ATPase and ATP-dependent Ca2+ transport activities in isolated plasma membranes of cold-acclimated and non-acclimated winter rye leaves (Secale cereale L. cv. Voima). Cold acclimation resulted in a two-fold higher Ca2+ transport activity, significantly different (P = 0.021) from that of non-acclimated rye, whereas only a small increase in H+ ATPase activity, measured as ATP hydrolysis, was observed in cold-acclimated compared to non-acclimated preparations. In plasma membranes, extensively washed with EDTA and Brij 58 to remove endogenous calmodulin, Ca2+ transport activity increased to about double by calmodulin addition, with both non-acclimated and cold-acclimated material. Uptake of Ca2+ was seen within the pHrange analyzed (pH 6–8), with an optimum at pH 7.2 with both materials, and both in the absence and in the presence of calmodulin. The increase in activity of ATP-dependent Ca2+ transport in cold-acclimated rye plasma membranes probably reflects the capacity needed to sustain the resting level of cytosolic Ca2+ concentration that is characteristic to the cold-acclimated situation.},
language = {en},
number = {3},
urldate = {2021-11-08},
journal = {Plant Physiology and Biochemistry},
author = {Puhakainen, Tuula and Pihakaski-Maunsbach, Kaarina and Widell, Susanne and Sommarin, Marianne},
month = mar,
year = {1999},
keywords = {Ca transport, Calmodulin, H ATPase, Secale cereale, cold acclimation, plasma membrane, rye},
pages = {231--239},
}
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Cold acclimation resulted in a two-fold higher Ca2+ transport activity, significantly different (P = 0.021) from that of non-acclimated rye, whereas only a small increase in H+ ATPase activity, measured as ATP hydrolysis, was observed in cold-acclimated compared to non-acclimated preparations. In plasma membranes, extensively washed with EDTA and Brij 58 to remove endogenous calmodulin, Ca2+ transport activity increased to about double by calmodulin addition, with both non-acclimated and cold-acclimated material. Uptake of Ca2+ was seen within the pHrange analyzed (pH 6–8), with an optimum at pH 7.2 with both materials, and both in the absence and in the presence of calmodulin. 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