@Article{biocell.2020.08242,
AUTHOR = {Yao SUN, Yao LI, Xin SUN, Qiong WU, Lei WANG},
TITLE = {Dephosphorylated mutations affect the protein-protein interactions of ERF in <i>Populus simonii x P. nigra</i>},
JOURNAL = {BIOCELL},
VOLUME = {44},
YEAR = {2020},
NUMBER = {1},
PAGES = {117--126},
URL = {http://www.techscience.com/biocell/v44n1/38431},
ISSN = {1667-5746},
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 <i>Populus simonii x Populus nigra</i>. 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 psnerf<sup>197/198/202a</sup> were predicted by homology modeling. The Y2H assay indicated that the deletion of
serine-rich regions does not affect the interactions, while dephosphorylated mutations blocked the interactions.
Homology modeling results suggested that the protein-binding activity was affected by dephosphorylation, and the
S197/S198/S202 residues of PsnERF may be the key phosphorylation sites influencing its binding ability.},
DOI = {10.32604/biocell.2020.08242}
}