Protein-serine/threonine kinases, myo-inositol-1-phosphate synthases and calmodulins, as the members of ABA and IP3/Ca2+ signal transduction pathway, played an important role in the low temperature stress.
Auxin responsive and transport protein, abscisic acid receptor, serine/threonine protein kinases and calmodulin were involved in signal transduction under low temperature stress.
In our experiment, 4 myo-inositol-1-phosphate synthase genes and 3 calmodulin genes participated in the resistance to low temperature stress, and the expression of calmodulin genes continued to increase during low temperature treatment.
The downstream components; mitogen-activated protein kinases, Hsp90 and calmodulins are involved in the activation of Heat-shock transcription factors (Hsf).
Among different classes of Ca2+ sensors calmodulin (CaM), calcineurin B-like proteins (CBLs) and CBL-interacting protein kinases (CIPKs), are the best characterized (Reddy et al., 2011; Yu et al., 2014).
It may transduce the signal to downstream transcription factors including Calmodulin Binding Transcription Activators (CAMTAs) (Pandey et al., 2013), GT-element-binding-like proteins (GTLs) (Weng et al., 2012) and MYBs (Yoo et al., 2005; Xie et al., 2014).
Gruissem, "Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants," Plant Cell, vol.
Braam, "Calmodulins and related potential calcium sensors of Arabidopsis," New Phytologist, vol.
Galaud, "Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals," Plant Signaling & Behavior, vol.
Several families of [Ca.sup.2+] sensors have been identified in higher plants based on the presence of EF-hand motifs including calmodulin proteins (CaMs) and calmodulin-like proteins (CMLs), calcineurin B-like proteins (CBLs), and [Ca.sup.2+]-dependent protein kinases (CPKs) [4, 5, 7-12].
Ranty, "Calmodulin and calmodulin-like proteins in plant calcium signaling," Biochimie, vol.
Yoo et al., "WRKY group IId transcription factors interact with calmodulin," FEBS Letters, vol.