scholarly journals Homospermidine biosynthesis in the cyanobacteriumAnabaenarequires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth

2018 ◽  
Vol 109 (6) ◽  
pp. 763-780 ◽  
Author(s):  
Mireia Burnat ◽  
Bin Li ◽  
Sok Ho Kim ◽  
Anthony J. Michael ◽  
Enrique Flores
Keyword(s):  
Deoxyhypusine Synthase ◽  
Diazotrophic Growth

scholarly journals Hypusination, a Metabolic Posttranslational Modification of eIF5A in Plants during Development and Environmental Stress Responses

Plants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1261
Author(s):  
Péter Pálfi ◽  
László Bakacsy ◽  
Henrietta Kovács ◽  
Ágnes Szepesi
Keyword(s):  
Amino Acid ◽  
Environmental Stress ◽  
Plant Development ◽  
Stress Responses ◽  
Posttranslational Modification ◽  
Proper Function ◽  
Signal Pathways ◽  
Deoxyhypusine Synthase ◽  
Deoxyhypusine Hydroxylase ◽  
Eukaryotic Translation

Hypusination is a unique posttranslational modification of eIF5A, a eukaryotic translation factor. Hypusine is a rare amino acid synthesized in this process and is mediated by two enzymes, deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). Despite the essential participation of this conserved eIF5A protein in plant development and stress responses, our knowledge of its proper function is limited. In this review, we demonstrate the main findings regarding how eIF5A and hypusination could contribute to plant-specific responses in growth and stress-related processes. Our aim is to briefly discuss the plant-specific details of hypusination and decipher those signal pathways which can be effectively modified by this process. The diverse functions of eIF5A isoforms are also discussed in this review.

Polysome-seq as a Measure of Translational Profile from Deoxyhypusine Synthase Mutant in Saccharomyces cerevisiae

2020 ◽  
pp. 168-179
Author(s):  
Fernanda Manaia Demarqui ◽  
Ana Carolina Silva Paiva ◽  
Mariana Marchi Santoni ◽  
Tatiana Faria Watanabe ◽  
Sandro Roberto Valentini ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Deoxyhypusine Synthase

scholarly journals Inactivation of a Heterocyst-Specific Invertase Indicates a Principal Role of Sucrose Catabolism in Heterocysts of Anabaena sp.

2010 ◽  
Vol 192 (20) ◽  
pp. 5526-5533 ◽  
Author(s):  
Rocío López-Igual ◽  
Enrique Flores ◽  
Antonia Herrero
Keyword(s):  
Fluorescent Protein ◽  
Northern Analysis ◽  
Filamentous Cyanobacterium ◽  
Nitrogen Deprivation ◽  
Vegetative Cells ◽  
Anabaena Sp ◽  
Green Fluorescent ◽  
Pcc 7120 ◽  
Diazotrophic Growth

ABSTRACT Anabaena sp. strain PCC 7120 is a filamentous cyanobacterium that carries out N2 fixation in specialized cells called heterocysts, which exchange nutrients and regulators with the filament's vegetative cells that perform the photosynthetic fixation of CO2. The Anabaena genome carries two genes coding for alkaline/neutral invertases, invA and invB. As shown by Northern analysis, both genes were expressed monocistronically and induced under nitrogen deprivation, although induction was stronger for invB than for invA. Whereas expression of an InvA-N-GFP fusion (green fluorescent protein [GFP] fused to the N terminus of the InvA protein [InvA-N]) was homogeneous along the cyanobacterial filament, consistent with the lack of dependence on HetR, expression of an InvB-N-GFP fusion upon combined nitrogen deprivation took place mainly in differentiating and mature heterocysts. In an hetR genetic background, the InvB-N-GFP fusion was strongly expressed all along the filament. An insertional mutant of invA could grow diazotrophically but was impaired in nifHDK induction and exhibited an increased frequency of heterocysts, suggesting a regulatory role of the invertase-mediated carbon flux in vegetative cells. In contrast, an invB mutant was strongly impaired in diazotrophic growth, showing a crucial role of sucrose catabolism mediated by the InvB invertase in the heterocysts.

Disruption of the Gene trx-m1 Impedes the Growth of Anabaena sp. PCC 7120 under Nitrogen Starvation

2019 ◽  
Vol 60 (7) ◽  
pp. 1504-1513 ◽  
Author(s):  
Fr�d�ric Deschoenmaeker ◽  
Shoko Mihara ◽  
Tatsuya Niwa ◽  
Hideki Taguchi ◽  
Jiro Nomata ◽  
...  
Keyword(s):  
Mutant Strain ◽  
Cellular Structure ◽  
Nitrogen Starvation ◽  
Nitrogen Response ◽  
Regulation Network ◽  
Anabaena Sp ◽  
Thiol Redox ◽  
Weak Expression ◽  
Pcc 7120 ◽  
Diazotrophic Growth

Abstract Cyanobacteria possess a sophisticated photosynthesis-based metabolism with admirable plasticity. This plasticity is possible via the deep regulation network, the thiol-redox regulations operated by thioredoxin (hereafter, Trx). In this context, we characterized the Trx-m1-deficient mutant strain of Anabaena sp., PCC 7120 (shortly named A.7120), cultivated under nitrogen limitation. Trx-m1 appears to coordinate the nitrogen response and its absence induces large changes in the proteome. Our data clearly indicate that Trx-m1 is crucial for the diazotrophic growth of A.7120. The lack of Trx-m1 resulted in a large differentiation of heterocysts (>20% of total cells), which were barely functional probably due to a weak expression of nitrogenase. In addition, heterocysts of the mutant strain did not display the usual cellular structure of nitrogen-fixative cells. This unveiled why the mutant strain was not able to grow under nitrogen starvation.

scholarly journals Extracellular signal-regulated kinases associate with and phosphorylate DHPS to promote cell proliferation

Oncogenesis ◽  
2020 ◽  
Vol 9 (9) ◽  
Author(s):  
Chao Wang ◽  
Zhen Chen ◽  
Litong Nie ◽  
Mengfan Tang ◽  
Xu Feng ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Lung Adenocarcinoma ◽  
Poor Prognosis ◽  
Protein Translation ◽  
Deoxyhypusine Synthase ◽  
Promote Cell Proliferation ◽  
Cellular Processes ◽  
Extracellular Signal ◽  
Direct Binding ◽  
Kinase Substrates

Abstract The ERK1/2 pathway is one of the most commonly dysregulated pathways in human cancers and controls many vital cellular processes. Although many ERK1/2 kinase substrates have been identified, the diversity of ERK1/2 mediated processes suggests the existence of additional targets. Here, we identified Deoxyhypusine synthase (DHPS), an essential hypusination enzyme regulating protein translation, as a major and direct-binding protein of ERK1/2. Further experiments showed that ERK1/2 phosphorylate DHPS at Ser-233 site. The Ser-233 phosphorylation of DHPS by ERK1/2 is important for its function in cell proliferation. Moreover, we found that higher DHPS expression correlated with poor prognosis in lung adenocarcinoma and increased resistance to inhibitors of the ERK1/2 pathway. In summary, our results suggest that ERK1/2-mediated DHPS phosphorylation is an important mechanism that underlies protein translation and that DHPS expression is a potent biomarker of response to therapies targeting ERK1/2-pathway.

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