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Buzeli, Reginaldo A.A.; Cascardo, Júlio Cézar M.; Rodrigues, Leonardo Augusto Zebral; Andrade, Maxuel O.; Almeida, Raul Santin; Loureiro, Marcelo Ehlers; Otoni, Wagner Campos; Fontes, Elizabeth P. B.

doi:10.1023/a:1019994721545

Cited by 37 publications

(14 citation statements)

References 44 publications

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“…For the second reporter gene construct, the 1000-, 700-, and 350-bp GmNRP-B promoter fragments were excised from TOPO-pCR4 with EcoRI-SalI digestion and cloned into the pLacZi integrative vector, a URA -marked plasmid, in front of the lacZ reporter gene under the control of a minimal, inactive CYC1 (cytochrome C1) promoter, resulting in pUFV1463, pUFV1464, and pUFV1465, respectively. A 350-bp fragment of the GmBiPD promoter was obtained from the clone pUFV228 (16) by digestion with EcoRI and SalI restriction enzymes and cloned into the pLacZi vector to be used as a negative control. The resulting clone, pUFV1226, contains the lacZ reporter gene under the control of an active soyBiPD promoter (16).…”

Section: Methodsmentioning

confidence: 99%

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A Novel Transcription Factor, ERD15 (Early Responsive to Dehydration 15), Connects Endoplasmic Reticulum Stress with an Osmotic Stress-induced Cell Death Signal

Alves

Reis

Dadalto³

et al. 2011

Journal of Biological Chemistry

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As in all other eukaryotic organisms, endoplasmic reticulum (ER) stress triggers the evolutionarily conserved unfolded protein response in soybean, but it also communicates with other adaptive signaling responses, such as osmotic stress-induced and ER stress-induced programmed cell death. These two signaling pathways converge at the level of gene transcription to activate an integrated cascade that is mediated by N-rich proteins (NRPs). Here, we describe a novel transcription factor, GmERD15 (Glycine max Early Responsive to Dehydration 15), which is induced by ER stress and osmotic stress to activate the expression of NRP genes. GmERD15 was isolated because of its capacity to stably associate with the NRP-B promoter in yeast. It specifically binds to a 187-bp fragment of the NRP-B promoter in vitro and activates the transcription of a reporter gene in yeast. Furthermore, GmERD15 was found in both the cytoplasm and the nucleus, and a ChIP assay revealed that it binds to the NRP-B promoter in vivo. Expression of GmERD15 in soybean protoplasts activated the NRP-B promoter and induced expression of the NRP-B gene. Collectively, these results support the interpretation that GmERD15 functions as an upstream component of stress-induced NRP-B-mediated signaling to connect stress in the ER to an osmotic stress-induced cell death signal.

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Section: Methodsmentioning

confidence: 99%

“…A 350-bp fragment of the GmBiPD promoter was obtained from the clone pUFV228 (16) by digestion with EcoRI and SalI restriction enzymes and cloned into the pLacZi vector to be used as a negative control. The resulting clone, pUFV1226, contains the lacZ reporter gene under the control of an active soyBiPD promoter (16). …”

Section: Methodsmentioning

confidence: 99%

A Novel Transcription Factor, ERD15 (Early Responsive to Dehydration 15), Connects Endoplasmic Reticulum Stress with an Osmotic Stress-induced Cell Death Signal

Alves

Reis

Dadalto³

et al. 2011

Journal of Biological Chemistry

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“…cis -elements analogous to mammalian ERSE, ERSE II and UPRE are also found in plant promoters, such as pERSE (CCAAT-N10-CACG), pUPRE (ATTGGTCCACGTCATC) and pUPRE-II (GATGACGCGTAC), and were found to be important for ER stress-induced gene expression [72,84–86]. …”

Section: Unfolded Protein Response (Upr)mentioning

confidence: 99%

Endoplasmic Reticulum (ER) Stress Response and Its Physiological Roles in Plants

Deng¹,

Srivastava²,

Howell³

2013

IJMS

100

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The endoplasmic reticulum (ER) stress response is a highly conserved mechanism that results from the accumulation of unfolded or misfolded proteins in the ER. The response plays an important role in allowing plants to sense and respond to adverse environmental conditions, such as heat stress, salt stress and pathogen infection. Since the ER is a well-controlled microenvironment for proper protein synthesis and folding, it is highly susceptible to stress conditions. Accumulation of unfolded or misfolded proteins activates a signaling pathway, called the unfolded protein response (UPR), which acts to relieve ER stress and, if unsuccessful, leads to cell death. Plants have two arms of the UPR signaling pathway, an arm involving the proteolytic processing of membrane-associated basic leucine zipper domain (bZIP) transcription factors and an arm involving RNA splicing factor, IRE1, and its mRNA target. These signaling pathways play an important role in determining the cell’s fate in response to stress conditions.

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“…S1). In addition, UPR-responsive cis -elements (UPRE-I, UPRE-III, ERSE-I, and ERSE-II) (Buzeli et al 2002; Hayashi et al 2013; Sun et al 2013) were identified in the promoter region for all three BdBiP genes ( BdBiP1, BdBip2, and BdBip3 ; Table 1). …”

Section: Resultsmentioning

confidence: 99%

In Brachypodium a complex signaling is actuated to protect cells from proteotoxic stress and facilitate seed filling

Kim

Zemelis-Durfee

Wilkerson

et al. 2017

Planta

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A conserved UPR machinery is required for Brachypodium ER stress resistance and grain filling. Human and livestock diets depend on the accumulation of cereal storage proteins and carbohydrates, including mixed-linkage glucan (MLG), in the endosperm during seed development. Storage proteins and proteins responsible for the production of carbohydrates are synthesized in the endoplasmic reticulum (ER). Unfavorable conditions during growth that hamper the ER biosynthetic capacity, such as heat, can cause a potentially lethal condition known as ER stress, which activates the unfolded protein response (UPR), a signaling response designed to mitigate ER stress. The UPR relies primarily on a conserved ER-associated kinase and ribonuclease, IRE1, which splices the mRNA of a transcription factor (TF), such as bZIP60 in plants, to produce an active TF that controls the expression of ER resident chaperones. Here, we investigated activation of the UPR in Brachypodium, as a model to study the UPR in seeds of a monocotyledon species, as well as the consequences of heat stress on MLG deposition in seeds. We identified a Brachypodium bZIP60 orthologue and determined a positive correlation between bZIP60 splicing and ER stress induced by chemicals and heat. Each stress condition led to transcriptional modulation of several BiP genes, supporting the existence of condition-specific BiP regulation. Finally, we found that the UPR is elevated at the early stage of seed development and that MLG production is negatively affected by heat stress via modulation of MLG synthase accumulation. We propose that successful accomplishment of seed filling is strongly correlated with the ability of the plant to sustain ER stress via the UPR.

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Cited by 37 publications

References 44 publications

A Novel Transcription Factor, ERD15 (Early Responsive to Dehydration 15), Connects Endoplasmic Reticulum Stress with an Osmotic Stress-induced Cell Death Signal

A Novel Transcription Factor, ERD15 (Early Responsive to Dehydration 15), Connects Endoplasmic Reticulum Stress with an Osmotic Stress-induced Cell Death Signal

Endoplasmic Reticulum (ER) Stress Response and Its Physiological Roles in Plants

In Brachypodium a complex signaling is actuated to protect cells from proteotoxic stress and facilitate seed filling

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