Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
Mais filtros











Base de dados
Intervalo de ano de publicação
1.
Nat Commun ; 15(1): 4881, 2024 Jun 07.
Artigo em Inglês | MEDLINE | ID: mdl-38849358

RESUMO

N6-methyladenosine (m6A) plays critical roles in regulating mRNA metabolism. However, comprehensive m6A methylomes in different plant tissues with single-base precision have yet to be reported. Here, we present transcriptome-wide m6A maps at single-base resolution in different tissues of rice and Arabidopsis using m6A-SAC-seq. Our analysis uncovers a total of 205,691 m6A sites distributed across 22,574 genes in rice, and 188,282 m6A sites across 19,984 genes in Arabidopsis. The evolutionarily conserved m6A sites in rice and Arabidopsis ortholog gene pairs are involved in controlling tissue development, photosynthesis and stress response. We observe an overall mRNA stabilization effect by 3' UTR m6A sites in certain plant tissues. Like in mammals, a positive correlation between the m6A level and the length of internal exons is also observed in plant mRNA, except for the last exon. Our data suggest an active m6A deposition process occurring near the stop codon in plant mRNA. In addition, the MTA-installed plant mRNA m6A sites correlate with both translation promotion and translation suppression, depicting a more complicated regulatory picture. Our results therefore provide in-depth resources for relating single-base resolution m6A sites with functions in plants and uncover a suppression-activation model controlling m6A biogenesis across species.


Assuntos
Adenosina , Arabidopsis , Regulação da Expressão Gênica de Plantas , Oryza , RNA Mensageiro , Oryza/genética , Oryza/crescimento & desenvolvimento , Oryza/metabolismo , Arabidopsis/genética , Arabidopsis/metabolismo , Arabidopsis/crescimento & desenvolvimento , Adenosina/análogos & derivados , Adenosina/metabolismo , RNA Mensageiro/metabolismo , RNA Mensageiro/genética , Transcriptoma/genética , RNA de Plantas/genética , RNA de Plantas/metabolismo , Regiões 3' não Traduzidas/genética , Perfilação da Expressão Gênica/métodos , Estabilidade de RNA/genética , Éxons/genética , Códon de Terminação/genética
2.
J Colloid Interface Sci ; 658: 74-89, 2024 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-38100978

RESUMO

In this study, we present the successful development of a unique photo-Fenton catalyst, 1T-2H MoS2@TP/PPy (MTP), achieved through the coating of a copolymer of tea polyphenol (TP) and polypyrrole (PPy) onto the surface of heterophase molybdenum disulfide (1T-2H MoS2). This innovative approach involves the integration of hydrothermal synthesis with copolymerization techniques. Our strategy utilizes nanoflower-like 1T-2H MoS2 as the foundational framework, which is then enveloped in TP and PPy copolymer. This innovative approach involves the integration of hydrothermal synthesis with copolymerization techniques. Our strategy utilizes nanoflower-like 1T-2H MoS2 as the foundational framework, which is then enveloped in TP and PPy copolymer. This distinctive architecture demonstrates exceptional catalytic performance owing to the hetero-phase entanglement of 1T-2H MoS2, which provides a diverse array of active sites. The coupled structure of TP and iron (TP-Fe2+/Fe3+) effectively overcome the limitation associated with the iron source. The incorporation of PPy not only reduces the recombination of photogenerated electron-hole pairs but also enhances the stability of 1T-2H MoS2. Remarkably, our experiments on the degradation of methylene blue (MB) and tetracycline (TC) degradation demonstrate that TP-Fe2+/Fe3+ significantly expands the pH applicability range of the MTP composite catalyst. Additionally, we examine several factors, including different catalysts, H2O2 addition, variations in light intensity, solution pH, temperature fluctuations, and the role of active species, to comprehensively understand their impact on the photo-Fenton degradation process. In conclusion, MTP composite exhibits robust catalytic stability and demonstrates a broad pH utilization range in the photo-Fenton oxidation process, highlighting its promising potential for a wide range of applications.

3.
Nat Plants ; 9(12): 2042-2058, 2023 12.
Artigo em Inglês | MEDLINE | ID: mdl-38066290

RESUMO

Light regulates chlorophyll homeostasis and photosynthesis via various molecular mechanisms in plants. The light regulation of transcription and protein stability of nuclear-encoded chloroplast proteins have been extensively studied, but how light regulation of mRNA metabolism affects abundance of nuclear-encoded chloroplast proteins and chlorophyll homeostasis remains poorly understood. Here we show that the blue light receptor cryptochrome 2 (CRY2) and the METTL16-type m6A writer FIONA1 (FIO1) regulate chlorophyll homeostasis in response to blue light. In contrast to the CRY2-mediated photo-condensation of the mRNA adenosine methylase (MTA), photoexcited CRY2 co-condenses FIO1 only in the presence of the CRY2-signalling protein SUPPRESSOR of PHYTOCHROME A (SPA1). CRY2 and SPA1 synergistically or additively activate the RNA methyltransferase activity of FIO1 in vitro, whereas CRY2 and FIO1, but not MTA, are required for the light-induced methylation and translation of the mRNAs encoding multiple chlorophyll homeostasis regulators in vivo. Our study demonstrates that the light-induced liquid-liquid phase separation of the photoreceptor/writer complexes is commonly involved in the regulation of photoresponsive changes of mRNA methylation, whereas the different photo-condensation mechanisms of the CRY/FIO1 and CRY/MTA complexes explain, at least partially, the writer-specific functions in plant photomorphogenesis.


Assuntos
Proteínas de Arabidopsis , Arabidopsis , Homeostase , Arabidopsis/genética , Arabidopsis/metabolismo , Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Proteínas de Ciclo Celular/metabolismo , Clorofila/metabolismo , Proteínas de Cloroplastos/metabolismo , Criptocromos/genética , Criptocromos/metabolismo , Regulação da Expressão Gênica de Plantas , Luz , Fatores de Transcrição/metabolismo , RNA Mensageiro/metabolismo , Metilação de RNA
4.
Nat Plants ; 7(10): 1397-1408, 2021 10.
Artigo em Inglês | MEDLINE | ID: mdl-34650267

RESUMO

Cryptochromes (CRYs) are photoreceptors that mediate light regulation of the circadian clock in plants and animals. Here we show that CRYs mediate blue-light regulation of N6-methyladenosine (m6A) modification of more than 10% of messenger RNAs in the Arabidopsis transcriptome, especially those regulated by the circadian clock. CRY2 interacts with three subunits of the METTL3/14-type N6-methyladenosine RNA methyltransferase (m6A writer): MTA, MTB and FIP37. Photo-excited CRY2 undergoes liquid-liquid phase separation (LLPS) to co-condense m6A writer proteins in vivo, without obviously altering the affinity between CRY2 and the writer proteins. mta and cry1cry2 mutants share common defects of a lengthened circadian period, reduced m6A RNA methylation and accelerated degradation of mRNA encoding the core component of the molecular oscillator circadian clock associated 1 (CCA1). These results argue for a photoregulatory mechanism by which light-induced phase separation of CRYs modulates m6A writer activity, mRNA methylation and abundance, and the circadian rhythms in plants.


Assuntos
Adenosina/análogos & derivados , Arabidopsis/genética , Relógios Circadianos/genética , Criptocromos/metabolismo , Fotorreceptores de Plantas/metabolismo , Adenosina/metabolismo , Arabidopsis/metabolismo , Arabidopsis/efeitos da radiação
5.
ACS Infect Dis ; 6(11): 2970-2978, 2020 11 13.
Artigo em Inglês | MEDLINE | ID: mdl-32946224

RESUMO

The pandemic outbreak of a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has threatened the global public health and economy since late December 2019. SARS-CoV-2 encodes the conserved macro domain within nonstructural protein 3, which may reverse cellular ADP-ribosylation and potentially cut the signal of a viral infection in the cell. Herein, we report that the SARS-CoV-2 macro domain was examined as a poly-ADP-ribose (ADPR) binding module and possessed mono-ADPR cleavage enzyme activity. After confirming the ADPR binding ability via a biophysical approach, the X-ray crystal structure of the SARS-CoV-2 macro domain was determined and structurally compared with those of other viruses. This study provides structural, biophysical, and biochemical bases to further evaluate the role of the SARS-CoV-2 macro domain in the host response via ADP-ribose binding but also as a potential target for drug design against COVID-19.


Assuntos
Betacoronavirus/metabolismo , Infecções por Coronavirus/virologia , Pneumonia Viral/virologia , Proteínas não Estruturais Virais/química , Proteínas não Estruturais Virais/metabolismo , Adenosina Difosfato Ribose/metabolismo , Antivirais/farmacologia , COVID-19 , Desenho de Fármacos , Humanos , Pandemias , Conformação Proteica , Domínios Proteicos , SARS-CoV-2
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA