Abstract

The sucrose non-fermentation-related protein kinase (SnRK) is a kind of Ser/Thr protein kinase, which plays a crucial role in plant stress response by phosphorylating the target protein to regulate the interconnection of various signaling pathways. However, little is known about the SnRK family in Eucalyptus grandis. Thirty-four putative SnRK sequences were identified in E. grandis and divided into three subgroups (SnRK1, SnRK2 and SnRK3) based on phylogenetic analysis and the type of domain. Chromosome localization showed that SnRK family members are unevenly distributed in the remaining 10 chromosomes, with the notable exception of chromosome 11. Gene structure analysis reveal that 10 of the 24 SnRK3 genes contained no introns. Moreover, conserved motif analyses showed that SnRK sequences belonged to the same subgroup that contained the same motif type of motif. The Ka/Ks ratio of 17 paralogues suggested that the EgrSnRK gene family underwent a purifying selection. The upstream region of EgrSnRK genes enriched with different type and numbers of cis-elements indicated that EgrSnRK genes are likely to play a role in the response to diverse stresses. Quantitative real-time PCR showed that the majority of the SnRK genes were induced by salt treatment. Genome-wide analyses and expression pattern analyses provided further understanding on the function of the SnRK family in the stress response to different environmental salt concentrations.

Highlights

  • Plants are confronted with various environmental insults in nature, such as drought, salt, low temperature and pathogen attack

  • Various studies have reported on protein kinase genes that are related to resistance, namely the receptor protein kinase (RLK) [3], mitogen-activated protein kinase (MAPK) [4], calcium dependent protein kinase (CDPK) [5], and sucrose nonfermenting1 (SNF1) kinase families [6]

  • SnRK3 can bind to calcineurin B-like (CBL) protein to participate in the Ca2+-mediated stress response, and is referred to as the calcineurin B-like protein-interacting protein kinases (CIPK)

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Summary

Introduction

Plants are confronted with various environmental insults in nature, such as drought, salt, low temperature and pathogen attack. Under these situations, plants are capable of initiating their own defense mechanism to adapt to various potentially stressful damaging challenges. The process of phosphorylation and dephosphorylation of proteins represents very important mechanisms for plants to respond to environmental stress signals [1]. Protein kinase is an important regulator in plants, which senses environmental signals through membrane receptor proteins and activates different protein phosphorylation pathways, which regulate the expression of downstream stress-resistant genes, and protect plants or reduce harm to those plants from an adverse external environment [2]. The N-terminal of CIPK has a conserved kinase domain and the C-terminal has two conserved domains: NAF and PPI [10,11]

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