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Updated: May 24, 2026

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Target deletion of the AAA ATPase PpCDC48II in Physcomitrella patens results in freezing sensitivity after cold
1College of Life Science, Capital Normal University, Beijing 100037, China. huiwangl@sina.com
Abstract:
CDC48 is a highly conserved protein in eukaryotes and belongs to the AAA (ATPase associated with a variety of cellular activities) superfamily. It can interact with many different co-factors and form protein complexes that play important roles in various cellular processes. According to the Physcomitrella patens database, one member of the ATPases, the cell cycle gene PpCDC48II, was cloned. PpCDC48II contains two typical ATPase modules and is highly homologous to AtCDC48A. PpCDC48II was up-regulated in mRNA levels after incubation at 0°C for 36 and 72 h. To further elucidate protein function, we disrupted the PpCDC48II gene by transforming P. patens with the corresponding linear genomic sequences. When treated to the same freezing stress, it was found that PpCDC48II knockout plants were less resistant to freezing treatment than wild type after acclimation. This suggested that PpCDC48II was an essential gene for low-temperature-induced freezing tolerance in P. patens cells.
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