Abstract

The homeodomain-leucine zipper (HD-Zip) gene family, as plant-specific transcription factors, plays an important role in plant development and growth as well as in the response to diverse stresses. Although HD-Zip genes have been extensively studied in many plants, they had not yet been studied in wheat, especially those involved in response to abiotic stresses. In this study, 46 wheat HD-Zip genes were identified using a genome-wide search method. Phylogenetic analysis classified these genes into four groups, numbered 4, 5, 17 and 20 respectively. In total, only three genes with A, B and D homoeologous copies were identified. Furthermore, the gene interaction networks found that the TaHDZ genes played a critical role in the regulatory pathway of organ development and osmotic stress. Finally, the expression profiles of the wheat HD-Zips in different tissues and under various abiotic stresses were investigated using the available RNA sequencing (RNA-Seq) data and then validated by quantitative real-time polymerase chain reaction (qRT-PCR) to obtain the tissue-specific and stress-responsive candidates. This study systematically identifies the HD-Zip gene family in wheat at the genome-wide level, providing important candidates for further functional analysis and contributing to the better understanding of the molecular basis of development and stress tolerance in wheat.

Highlights

  • The homeodomain-leucine zipper (HD-Zip) gene family is one of the key transcription factors in plants, playing a vital role in various abiotic stresses and signal transduction [1,2,3]

  • We identified and characterized the wheat HD-Zip gene family based on a genome-wide search approach

  • Results revealed that the HD-Zip genes were unevenly distributed on wheat chromosomes

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Summary

Introduction

The homeodomain-leucine zipper (HD-Zip) gene family is one of the key transcription factors in plants, playing a vital role in various abiotic stresses and signal transduction [1,2,3]. HD-Zip proteins possess the conserved HD domain, acting as a specific DNA binding site at the. C-terminal, together with the adjacent leucine-zipper (LZ) motif that is responsible for protein dimerization [4,5]. Based on the sequence homology, DNA binding specificity and physiological functioning, HD-Zip genes were further divided into four groups, namely HD-Zip I, II, III and IV [6]. Members of groups I and II interacted with similar DNA binding sites of the pseudo-palindromic sequence CAATNATTG [5,7]. CPSCE motif consisting of five conserved amino acids—Cys, Pro, Ser, Cys and Glu—which acted as a sensory domain to redox the cell state and were located downstream of the Zip domain [8,9].

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