Abstract
BackgroundFormin, a highly conserved multi-domain protein, interacts with microfilaments and microtubules. Although specifically expressed formin genes in anthers are potentially significant in research on male sterility and hybrid wheat breeding, similar reports in wheat, especially in thermo-sensitive genic male sterile (TGMS) wheat, remain elusive.ResultsHerein, we systematically characterized the formin genes in TGMS wheat line BS366 named TaFormins (TaFHs) and predicted their functions in inducing stress response. In total, 25 TaFH genes were uncovered, majorly localized in 2A, 2B, and 2D chromosomes. According to the neighbor-joining (NJ) method, all TaFH proteins from wheat and other plants clustered in 6 sub-groups (A-F). The modeled 3D structures of TaFH1-A/B, TaFH2-A/B, TaFH3-A/B and TaFH3-B/D were validated. And different numbers of stress and hormone-responsive regulatory elements in their 1500 base pair promoter regions were contained in the TaFH genes copies. TaFHs had specific temporal and spatial expression characteristics, whereby TaFH1, TaFH4, and TaFH5 were expressed highly in the stamen of BS366. Besides, the accumulation of TaFHs was remarkably lower in a low-temperature sterile condition (Nanyang) than fertile condition (Beijing), particularly at the early stamen development stage. The pollen cytoskeleton of BS366 was abnormal in the three stages under sterile and fertile environments. Furthermore, under different stress levels, TaFHs expression could be induced by drought, salt, abscisic acid (ABA), salicylic acid (SA), methyl jasmonate (MeJA), indole-3-acetic acid (IAA), polyethylene glycol (PEG), and low temperature. Some miRNAs, including miR167, miR1120, and miR172, interacts with TaFH genes; thus, we constructed an interaction network between microRNAs, TaFHs, phytohormone responses, and distribution of cytoskeleton to reveal the regulatory association between upstream genes of TaFH family members and sterile.ConclusionsCollectively, this comprehensive analysis provides novel insights into TaFHs and miRNA resources for wheat breeding. These findings are, therefore, valuable in understanding the mechanism of TGMS fertility conversion in wheat.
Highlights
Formin, a highly conserved multi-domain protein, interacts with microfilaments and microtubules
After identifying the formin genes of wheat (TaFHs), we evaluated their characteristics for the physicochemical, phylogenetic relationship, 3D structure, motif structure, exon/intro structure, chromosomal location, miRNA regulation, and expression patterns in different tissues and different development stages of anthers in the thermo-sensitive genic male sterile (TGMS) wheat line, BS366
Identifying formin genes in wheat Two strategies were adopted to mine for formin genes in T. aestivum L
Summary
A highly conserved multi-domain protein, interacts with microfilaments and microtubules. Formins (formin homology proteins), a group of proteins involved in actin polymerization, are associated with the fast-growing end (bared end) of actin filaments, potentially mediating a series of cellular functions, including polarity, division, cytokinesis, migration, among others. The formin proteins are characterized by two formin homology (FH) domains, FH1 and FH2. The FH1 (formin homology 1) domain harbors a distinct polyproline-rich region that binds to a crucial actin-binding proteinprofilin or actin/profilin complex. Profilin is a vital monomer actin-binding protein and can interact with formin via the FH1 domain. The FH2 (formin homology 2) domain is characterized by a key sequence that interacts with actin [2]. Plant formins occur in two categories, type I and type II, based on the sequence homology of their FH (formin homology) domains. Type I formins have a transmembrane (TM) domain at their N-terminus followed by the C-terminal FH1 and FH2 domains, whereas type II formins do not have an N-terminal TM domain but carry an N-terminal phosphatase and tensinrelated (PTEN)-like domain besides the conserved FH1 and FH2 domains [3]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
