Abstract
bZIP gene family is one of the largest transcription factor families. It plays an important role in plant growth, metabolic, and environmental response. However, complete genome-wide investigation of bZIP gene family in Glycyrrhiza uralensis remains unexplained. In this study, 66 putative bZIP genes in the genome of G. uralensis were identified. And their evolutionary classification, physicochemical properties, conserved domain, functional differentiation, and the expression level under different stress conditions were further analyzed. All the members were clustered into 13 subfamilies (A–K, M, and S). A total of 10 conserved motifs were found in GubZIP proteins. Members from the same subfamily shared highly similar gene structures and conserved domains. Tandem duplication events acted as a major driving force for the evolution of bZIP gene family in G. uralensis. Cis-acting elements and protein–protein interaction networks showed that GubZIPs in one subfamily are involved in multiple functions, while some GubZIPs from different subfamilies may share the same functional category. The miRNA network targeting GubZIPs showed that the regulation at the transcriptional level may affect protein–protein interaction networks. We suspected that domain-mediated interactions may categorize a protein family into subfamilies in G. uralensis. Furthermore, the tissue-specific gene expression patterns of GubZIPs were analyzed using the public RNA-seq data. Moreover, gene expression level of 66 bZIP family members under abiotic stress treatments was quantified by using qRT-PCR. The results of this study may serve as potential candidates for functional characterization in the future.
Highlights
Basic leucine zipper is a transcription factors (TFs) family and widely distributed in eukaryotes
A total of 66 members of GubZIP gene family were obtained from the genome of G. uralensis using a series of bioinformatics methods based on hidden Markov model (HMM)
The Basic leucine zipper (bZIP) gene family plays an important role in plant growth, development, and response to biotic and abiotic stress
Summary
Basic leucine zipper (bZIP) is a transcription factors (TFs) family and widely distributed in eukaryotes. The structure of bZIP protein is defined by the conserved bZIP protein and often acts as a dimer (Mair et al, 2015). The bZIP TF has a specific bZIP Gene Family in Licorice sequence consisting of a fixed motif N-X7-R/K and a leucine zipper that binds to the alkaline region. In the leucine zipper region, the highly conserved heptad repeats of leucine may be replaced by phenylalanine (F), valine (V), isoleucine (I), or methionine (M) and make bZIP protein form a variety of binding ways of homodimer and heterodimer. BZIP proteins preferentially combined with ACGT as the core motif to form a palindrome structure (Dröge-Laser et al, 2018) In the leucine zipper region, the highly conserved heptad repeats of leucine may be replaced by phenylalanine (F), valine (V), isoleucine (I), or methionine (M) and make bZIP protein form a variety of binding ways of homodimer and heterodimer. bZIP proteins preferentially combined with ACGT as the core motif to form a palindrome structure (Dröge-Laser et al, 2018)
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