Characterization of wheat Bell1-type homeobox genes in floral organs of alloplasmic lines with Aegilops crassa cytoplasm

Mizumoto, Kota; Hatano, Hitoshi; Hirabayashi, Chizuru; Murai, Koji; Takumi, Shigeo

doi:10.1186/1471-2229-11-2

Cited by 12 publications

(10 citation statements)

References 68 publications

(126 reference statements)

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“…These clones were sequenced and identified based on sequence similarity searches with BLASTN or BLASTX software at National Center for Biotechnology Information (NCBI) and The Institute for Genomic Research (TIGR) databases. The following proteins were identified: (1) WBLH1, a previously described wheat homeodomain protein (Mizumoto et al, 2011); (2) WVIP2 (Wilson et al, 2005), a protein sharing 93% amino acid similarity with the wild oat (Avena fatua) Viviparus1 Interacting Protein2 (VIP2; Jones et al, 2000); and (3) TdWNK5, a protein with 75% amino acid similarity to Arabidopsis With No Lys [K] 5 (AtWNK5), a member of the Arabidopsis WNK family of MAP kinases . Ubiquitination assay on TdRF1.…”

Section: Identification Of Tdrf1 Protein Interactorsmentioning

confidence: 99%

“…4), we demonstrated that the RING-finger protein TdRF1 interacts with WBLH1, TdWNK5, and WVIP2. The homotranscription factor WBLH1, previously isolated by Mizumoto et al (2011), is homologous to HvJuBEL1 (94% of amino acid similarity), which is involved in the control of leaf development (Mü ller et al, 2001) and is part of the BEL1-like protein family whose members are involved in various developmental aspects (Mizumoto et al, 2011). TdWNK5 is 75% similar to AtWNK5, a member of the Arabidopsis WNK family of MAP kinases .…”

Section: A Small Stress-related Interactome Around Tdrf1mentioning

confidence: 99%

“…The homeodomain WBLH1 protein is part of the small BEL1-like (BLH1) protein family, which belongs to the threeamino acid loop extension superfamily. BLH1s are transcription factors involved in various developmental aspects like seed shattering, ovule morphogenesis, and leaf shape establishment (Mizumoto et al, 2011). Many BLH1 proteins interact with the KNOTTED1-like homeobox (KNOX) transcription factors, which also belong to the three-amino acid loop extension superfamily (Bellaoui et al, 2001) and regulate morphogenesis (Hay and Tsiantis, 2010).…”

Section: Tdrf1 Mediates the 26s Proteasome Degradation Of The Transcrmentioning

confidence: 99%

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Identification of a Protein Network Interacting with TdRF1, a Wheat RING Ubiquitin Ligase with a Protective Role against Cellular Dehydration

et al. 2011

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Plants exploit ubiquitination to modulate the proteome with the final aim to ensure environmental adaptation and developmental plasticity. Ubiquitination targets are specifically driven to degradation through the action of E3 ubiquitin ligases. Genetic analyses have indicated wide functions of ubiquitination in plant life; nevertheless, despite the large number of predicted E3s, only a few of them have been characterized so far, and only a few ubiquitination targets are known. In this work, we characterized durum wheat (Triticum durum) RING Finger1 (TdRF1) as a durum wheat nuclear ubiquitin ligase. Moreover, its barley (Hordeum vulgare) homolog was shown to protect cells from dehydration stress. A protein network interacting with TdRF1 has been defined. The transcription factor WHEAT BEL1-TYPE HOMEODOMAIN1 (WBLH1) was degraded in a TdRF1-dependent manner through the 26S proteasome in vivo, the mitogen-activated protein kinase TdWNK5 [for Triticum durum WITH NO LYSINE (K)5] was able to phosphorylate TdRF1 in vitro, and the RING-finger protein WHEAT VIVIPAROUS-INTERACTING PROTEIN2 (WVIP2) was shown to have a strong E3 ligase activity. The genes coding for the TdRF1 interactors were all responsive to cold and/or dehydration stress, and a negative regulative function in dehydration tolerance was observed for the barley homolog of WVIP2. A role in the control of plant development was previously known, or predictable based on homology, for wheat BEL1-type homeodomain1(WBLH1). Thus, TdRF1 E3 ligase might act regulating the response to abiotic stress and remodeling plant development in response to environmental constraints.Plants are sessile organisms that must cope with their surrounding environments; thus, stresses such as drought, soil salinity, or extreme temperatures represent common events during their life cycle. These unfavorable conditions limit plant growth and development and strongly threat crop productivity, preventing the expression of the full genetic potential of cultivars. At the molecular level, upon plant exposition to stress, a plethora of genes are up-or down-regulated to reorganize the metabolic fluxes leading to plant adaptation as a final result. These responses provide plants with the capacity to avoid or mitigate the effects of stresses. Besides gene transcriptional changes, cells have evolved other types of molecular responses, such as posttranslational modifications of key proteins (Mazzucotelli et al., 2008). Among them, protein phosphorylation and ubiquitination are key components of the molecular response to different types of abiotic stresses. These modifications are implicated in signal transduction, positive and negative regulation of the response, and cross-connections between different signaling pathways and stress responses. The rapid and precise activation or inhibition of regulatory proteins is essential for the coordination of an array of physiological responses to cope with different stresses and to ensure a tightly controlled regulation of cellular changes induced by stress inte...

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Section: Identification Of Tdrf1 Protein Interactorsmentioning

confidence: 99%

Section: A Small Stress-related Interactome Around Tdrf1mentioning

confidence: 99%

Section: Tdrf1 Mediates the 26s Proteasome Degradation Of The Transcrmentioning

confidence: 99%

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Identification of a Protein Network Interacting with TdRF1, a Wheat RING Ubiquitin Ligase with a Protective Role against Cellular Dehydration

et al. 2011

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“…BLH form heterodimeric complexes with STM and BP. This KNOX-BLH interaction is conserved among various plant species (Mizumoto et al, 2011;Arnaud and Pautot, 2014;Sharma et al, 2014).…”

Section: Class 1 Knox Homeodomain Transcription Factorsmentioning

confidence: 99%

Plant development regulation: Overview and perspectives

Yruela

2015

Journal of Plant Physiology

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Plant development, as occur in other eukaryotes, is conducted through a complex network of hormones, transcription factors, enzymes and micro RNAs, among other cellular components.They control developmental processes such as embryo, apical root and shoot meristem, leaf, flower, or seed formation, among others. The research in these topics has been very active in last decades. Recently, an explosion of new data concerning regulation mechanisms as well as the response of these processes to environmental changes has emerged. Initially, most of investigations were carried out in the model eudicot Arabidopsis but currently data from other plant species are available in the literature, although they are still limited. The aim of this review is focused on the current knowledge of main molecular actors involved in plant development regulation in diverse plant species. A special attention will be given to the major families of genes and proteins participating in these mechanisms. The information on the regulatory pathways where they participate will be briefly cited. Additionally, he importance of certain structural features of such proteins that confer ductility and flexibility to these mechanisms will also be reported and discussed.

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“…TdRF1 guides to degradation the transcription factor WBLH1 whose barley homolog HvJuBEL1 controls leaf development. 5,6 TdRF1 is phosphorylated by TdWNK5 which belongs to the WNK family of kinases known to have a role in the control of flowering time. 7 For WVIP2 an interaction with the master regulator of embryo dormancy VP1 can be hypothesized based on its extensive homology with the Avena fatua Af VIP2.…”

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confidence: 99%

The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination

Guerra

Cattivelli

Mazzucotelli

2012

Plant Signaling & Behavior

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Determining the half-life of proteins, ubiquitination plays a fundamental role in the regulation of cellular processes through the proteasome-mediated protein degradation. Main actors of this theme are the E3 ubiquitin ligases which specifically recruit the protein targets for ubiquitination.1 Further, ubiquitination enzymes can crosstalk, providing an additional layer of ubiquitin-dependent control on cellular activities.The ubiquitin proteasome system strongly impacts on the signaling pathways of abiotic stress tolerance, including those dependent by ABA.2 The control of the E3 ligases on stress response can be exerted through the suppression of stress signaling pathways during favorable growth conditions, the degradation of negative regulators of stress response upon stress exposition, or the attenuation of stress signaling pathways for further growth once environmental conditions have improved. In a previous paper we showed that WVIP2 3 and TdRF1 are two RING finger proteins of durum wheat (Triticum durum) with a demonstrated ubiquitin ligases activity. 4 The corresponding genes are stress responsive, both upregulated upon cold treatment and downregulated by ABA, and with contrasting behavior in response to dehydration, with TdRF1 upregulated and WVIP2 downregulated. Further, transient induced gene silencing experiments suggested a positive and negative effect for TdRF1 and WVIP2, respectively, on tolerance to dehydration in vitro.Plant cells regulate many cellular processes controlling the half-life of critical proteins through ubiquitination. Previously, we characterized two interacting rinG-type E3 ubiquitin ligases of Triticum durum, tdrF1 and WViP2. We revealed their role in tolerance to dehydration, and existing knowledge about their partners also indicated their involvement in the regulation of some aspects of plant development. here we located WViP2 in the regulation of the aBa signaling, based on sequence similarities. Further we acquired general evidence about the versatility of ubiquitination in plant cells. a protein can be target of different E3 ligases for a perfect tuning of its abundance as well as the same E3 ligase can ubiquitinate different and unrelated proteins, thus representing a cross-connections between different signaling pathways for a global coordination of cellular processes.

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Characterization of wheat Bell1-type homeobox genes in floral organs of alloplasmic lines with Aegilops crassa cytoplasm

Cited by 12 publications

References 68 publications

Identification of a Protein Network Interacting with TdRF1, a Wheat RING Ubiquitin Ligase with a Protective Role against Cellular Dehydration

Identification of a Protein Network Interacting with TdRF1, a Wheat RING Ubiquitin Ligase with a Protective Role against Cellular Dehydration

Plant development regulation: Overview and perspectives

The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination

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