Yao SUN, Yao LI, Xin SUN, Qiong WU, Lei WANG*
BIOCELL, Vol.44, No.1, pp. 117-126, 2020, DOI:10.32604/biocell.2020.08242
- 01 March 2020
Abstract Phosphorylation is a common type of post-translational modification (PTM). It plays a vital role in many
cellular processes. The reversible phosphorylation and dephosphorylation affect protein structures and proteinprotein
interactions. Previously, we obtained five proteins that interact with ethylene-responsive factor (ERF) from the
cDNA library of Populus simonii x Populus nigra. To further investigate the effect of dephosphorylation of PsnERF on
its protein binding ability, we generated different phosphorylation states of PsnERF and demonstrated their protein
binding capacity by the yeast two-hybrid assay (Y2H). The secondary structures and 3D structures of PsnERF, ERFm,
TrunERF, and psnerf197/198/202a were predicted More >
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