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Biology subjects

Correa-Aragunde, N.

Publications and source records attributed to Correa-Aragunde, N..

4 recordsLinked to original sources

Nitric Oxide Modulates Auxin Signaling through TIR1 S-Nitrosylation During Thermomorphogenesis in Arabidopsis

Auxin, a central hormone coordinating plant growth, integrates both environmental and developmental signals to regulate cell expansion, division, and organ patterning. Among these environmental cues, elevated ambient temperatures trigger a suite of developmental adaptations collectively known as thermomorphogenesis. In this study, we identify nitric oxide (NO) as a key mediator in the temperature-dependent regulation of auxin signaling. Our results show that warm temperatures (28-29 {degrees}C) enhance auxin-induced NO accumulation in Arabidopsis thaliana seedlings. Using pharmacological and genetic approaches, we demonstrate that NO is required for proper thermomorphogenic responses in aerial tissues. This redox signal promotes the stabilization and nuclear localization of the F-box auxin receptor TIR1, a crucial step for the activation of downstream auxin responses. Specifically, tir1-1 seedlings expressing a non-nitrosylatable TIR1 variant mutated at the Cys140 residue exhibit impaired hypocotyl elongation and hyponasty under warm conditions compared to seedlings complemented with wild-type TIR1. These results highlight the functional relevance of the TIR1 Cys140 residue, a known target for S-nitrosylation, in coordinating thermomorphogenic responses. In contrast, the absence of TIR1 S-nitrosylation restricts primary root elongation at 22 {degrees}C but does not affect the growth-promoting effects of warm temperatures. Our findings uncover a novel redox-dependent regulatory layer in auxin signaling, where S-nitrosylation of TIR1 may modulate its stability and subcellular localization in a temperature- and organ-specific manner. This mechanism allows differential growth responses between shoot and root organs and highlights the complexity of hormonal and redox interplay during plant adaptation to elevated temperatures.

plant biology↗

A bifunctional CPD/(6-4)- photolyase from the cyanobacteria Synechococcus sp. PCC 7335 constitutes an UV-B inducible operon: new insights into photolyases phylogenetic evolution

Photosynthetic organisms are continuously exposed to solar ultraviolet radiation-B (UV-B) because of their autotrophic lifestyle. UV-B provokes DNA damages, as cyclobutane pyrimidine dimers (CPD) or pyrimidine (6-4) pyrimidone photoproducts (6-4 PPs). The cryptochrome/ photolyase family (CPF) comprises flavoproteins that are able to bind damaged or undamaged DNA. Photolyases (PHRs) are enzymes that repair either CPDs or 6-4 PPs. A natural bifunctional CPD/(6-4)- PHR (PhrSph98) was recently isolated from the UV-resistant bacteria Sphingomonas UV9. In this work, phylogenetic studies of bifunctional CPD/(6-4)- photolyases and its evolutionary relationship with other CPF members were performed. Amino acids involved in electron transfer and binding to FAD cofactor and DNA lesions were conserved in proteins from proteobacteria, planctomycete, bacteroidete, acidobacteria and cyanobacteria clades. Genome analysis revealed that the cyanobacteria Synechococcus sp. PCC 7335 encodes a two-gene assembly operon coding for a PHR and a bifunctional CPD/(6-4)- PHR. Operon structure was validated by RT-qPCR analysis and the polycistronic transcript accumulated after 15 minutes of UV-B irradiation. Conservation of structure and evolution is discussed. This is the first report of an UV-B inducible PHRs operon which encodes a CPD/(6-4)- photolyase with putative bifunctional role in the repair of CPDs and 6-4 PPs damages in oxygenic photosynthetic organisms.

evolutionary biology↗

Nitric oxide synthases from photosynthetic organisms improve growth and confer nitrosative stress tolerance in E. coli. Insights on the pterin cofactor

Nitric oxide synthase (NOS) synthesizes NO from the substrate L-arginine (Arg). NOS with distinct biochemical properties were characterized from two photosynthetic microorganisms, the unicellular algae Ostreococcus tauri (OtNOS) and the cyanobacteria Synechococcus PCC 7335 (SyNOS). In this work we studied OtNOS and SyNOS recombinantly expressed in E. coli and analyzed bacterial growth and tolerance to nitrosative stress. Results show that the expression of OtNOS and SyNOS promotes bacterial growth and allows metabolizing Arg as N source. In accordance to a high NO producing activity, OtNOS expression induces the hmp flavohemoglobin in E. coli, suggesting that this strain is sensing nitrosative stress. The addition of 1 mM of the NO donor sodium nitroprusside (SNP) is toxic and generates a strong nitrosative stress. The expression of OtNOS or SyNOS reduced SNP toxicity restoring bacterial growth. Finally, using bioinformatic tools and ligand docking analyses, we propose tetrahydromonapterin (MH4), an endogenous pterin found in E. coli, as potential cofactor required for NOS catalytic activity. Our findings could be useful for the development of biotechnological applications using NOS expression to improve growth in bacteria. Key points- The NO synthase (NOS) from photosynthetic microorganisms were expressed in E. coli - Expression of NOS increases bacterial growth and tolerance to nitrosative stress. - Ligand docking analyses indicate tetrahydromonapterin (MH4) as potential NOS cofactor in E. coli.

microbiology↗

Cyanobacterial NOS expression improves nitrogen use efficiency, nitrogen-deficiency tolerance and yield in Arabidopsis

Developing strategies to improve nitrogen (N) use efficiency (NUE) in plants is a challenge to reduce environmental problems linked to over-fertilization. The nitric oxide synthase (NOS) enzyme from the cyanobacteria Synechococcus PCC 7335 (SyNOS) has been recently identified and characterized. SyNOS catalyzes the conversion of arginine to citrulline and nitric oxide (NO), and then 70% of the produced NO is rapidly oxidized to nitrate by an unusual globin domain in its 5'-terminus. In this study, we assessed whether SyNOS expression in plants affects N metabolism improving NUE and yield. Our results showed that transgenic Arabidopsis plants had higher primary shoot length and shoot branching when grown in N-deficient conditions and higher seed production in N-sufficient and -deficient conditions. Moreover, transgenic plants showed significantly increased NUE in both N conditions. No differences were observed in N uptake for SyNOS lines. However, SyNOS lines presented an increase in N assimilation/remobilization under low N conditions. In addition, SyNOS lines had greater N-deficiency tolerance compared to wt plants. Our results support that SyNOS expression generates a positive effect on N metabolism and seed production in Arabidopsis, and it might be envisaged as a strategy to improve productivity in crops under adverse N environments.

plant biology↗