Open Access

ARTICLE

Dephosphorylated mutations affect the protein-protein interactions of ERF in Populus simonii x P. nigra

by Yao SUN, Yao LI, Xin SUN, Qiong WU, Lei WANG

Institute of Advanced Technology, Heilongjiang Academy of Sciences, Harbin, China

* Address correspondence to: Lei Wang,

BIOCELL 2020, 44(1), 117-126. https://doi.org/10.32604/biocell.2020.08242

Issue published 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 psnerf^197/198/202a 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.

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