The plant UV-B photoreceptor UV RESISTANCE LOCUS 8(UVR8)exists as a homodimer in its inactive ground state.Upon UV-B exposure,UVR8monomerizes and interacts with a downstreamkey regulator,theCONSTITUTIVE PHOTOMORPHOGEN...The plant UV-B photoreceptor UV RESISTANCE LOCUS 8(UVR8)exists as a homodimer in its inactive ground state.Upon UV-B exposure,UVR8monomerizes and interacts with a downstreamkey regulator,theCONSTITUTIVE PHOTOMORPHOGENIC 1/SUPPRESSOR OF PHYA(COP1/SPA)E3 ubiquitin ligase complex,to initiate UV-B signaling.Two WD40 proteins,REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1(RUP1)and RUP2 directly interact with monomeric UVR8 and facilitate UVR8 ground state reversion,completing the UVR8 photocycle.Here,we reconstituted the RUP-mediated UVR8 redimerization process in vitro and reported the structure of the RUP2-UVR8^(W285A) complex(2.0A).RUP2 and UVR8^(W285A) formed a heterodimer via two distinct interfaces,designated Interface 1 and 2.The previously characterized Interface 1 is found between the RUP2 WD40 domain and the UVR8 C27 subregion.The newly identified Interface 2 is formed through interactions between the RUP2 WD40 domain and the UVR8 core domain.Disruption of Interface 2 impairedUV-B induced photomorphogenic development in Arabidopsis thaliana.Further biochemical analysis indicated that both interfaces are important for RUP2-UVR8 interactions and RUP2-mediated facilitation of UVR8 redimerization.Our findings suggest that the two-interface-interaction mode is adopted by both RUP2 and COP1 when they interact with UVR8,marking a step forward in understanding the molecular basis that underpins the interactions between UVR8 and its photocycle regulators.展开更多
Plants have evolved and perfected a series of light receptors to feel the light at different bands and regulate the expression, modification and interaction of related genes in plants through signal transduction. So f...Plants have evolved and perfected a series of light receptors to feel the light at different bands and regulate the expression, modification and interaction of related genes in plants through signal transduction. So far, many photoreceptors have been identified in plants, UVR8 has recently been identified as a receptor for UV-B light. This paper cloned a WD40 gene related to UVR8 protein subunit, named RrRUP2, based on the Rosa rugose transcriptome data, using Rosa rugose “Zi zhi” as experimental materials. The full length of cDNA of the gene was obtained by RT-PCR and RACE methods. The total length of this gene is 1173 bp, and it encodes 390 amino acids. After bioinformatics analysis, the molecular formula C3415H5659N1173O1434S313 was predicted;the relative molecular weight was 96129.27 Da;the theoretical isoelectric point PI value was 5.00;and its instability index was 47.06. The total average hydrophobic index was 0.750. In the secondary structure of RrRUP2 protein, there are 10 α-helix, 45 β-helix, 181 Random coil, and 154 Extended strand. Gene Bank Blast results showed that the amino acid sequence encoded by RrRUP2 was more than 90% homologous with the RUP2 protein of Rosa chinensis, Fragaria, Malus, Pyrus, Prunus, Juglans, Arabidopsis and Tobacco, so it can be inferred that the RrRUP2 gene is a WD repeat-containing protein. Regarding to fluorescence quantitative expression analysis of RrRUP2, we find its experssion pattern is corresponded with the accumulation of anthocyanins.展开更多
Developing efficient and stable catalysts for the hydrogen evolution reaction(HER)is essential for advancing anion-exchange membrane water electrolyzer(AEMWE)technology.In this study,we present a facile microwave redu...Developing efficient and stable catalysts for the hydrogen evolution reaction(HER)is essential for advancing anion-exchange membrane water electrolyzer(AEMWE)technology.In this study,we present a facile microwave reduction and low-temperature phosphorization strategy to synthesize a highly efficient HER catalyst,comprising P,N-codoped carbon-supported RuP_(2)nanocluster(RuP_(2)@PNC).RuP_(2)@PNC demonstrates outstanding HER performance,achieving overpotentials of 18 and 44 mV at a current density of 10 mA cm^(-2)in alkaline and acidic media,respectively.Furthermore,an AEMWE device utilizing RuP_(2)@PNC as the cathode catalyst delivers a current density of 0.5 A cm^(-2)at a cell voltage of 1.84 V and exhibits remarkable stability over 150 h of operation.Experimental analyses and density functional theory(DFT)calculations reveal that the synergistic effects of P,N-codoped and the unique structure of RuP_(2)enhance electron transfer between Ru and the support,optimize the electronic structure,and regulate the d–band center of Ru.These features improve water adsorption,weaken the Ru–H binding strength,and facilitate efficient H_(2)desorption,collectively driving the superior HER activity of RuP_(2)@PNC.This work offers an effective design strategy for high-performance HER catalysts and provides valuable insights for accelerating the development of AEMWE technology.展开更多
基金supported by funds from the National Key R&D Program of China(2018YFA0507700 and 2017YFA0506100)the National Natural Science Foundation of China(31722017,31870753,and 32122011)+1 种基金the Foundation of Hubei Hongshan Laboratory(2021hszd010)the China Postdoctoral Science Foundation(2020M682437 for Ling Ma).
文摘The plant UV-B photoreceptor UV RESISTANCE LOCUS 8(UVR8)exists as a homodimer in its inactive ground state.Upon UV-B exposure,UVR8monomerizes and interacts with a downstreamkey regulator,theCONSTITUTIVE PHOTOMORPHOGENIC 1/SUPPRESSOR OF PHYA(COP1/SPA)E3 ubiquitin ligase complex,to initiate UV-B signaling.Two WD40 proteins,REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1(RUP1)and RUP2 directly interact with monomeric UVR8 and facilitate UVR8 ground state reversion,completing the UVR8 photocycle.Here,we reconstituted the RUP-mediated UVR8 redimerization process in vitro and reported the structure of the RUP2-UVR8^(W285A) complex(2.0A).RUP2 and UVR8^(W285A) formed a heterodimer via two distinct interfaces,designated Interface 1 and 2.The previously characterized Interface 1 is found between the RUP2 WD40 domain and the UVR8 C27 subregion.The newly identified Interface 2 is formed through interactions between the RUP2 WD40 domain and the UVR8 core domain.Disruption of Interface 2 impairedUV-B induced photomorphogenic development in Arabidopsis thaliana.Further biochemical analysis indicated that both interfaces are important for RUP2-UVR8 interactions and RUP2-mediated facilitation of UVR8 redimerization.Our findings suggest that the two-interface-interaction mode is adopted by both RUP2 and COP1 when they interact with UVR8,marking a step forward in understanding the molecular basis that underpins the interactions between UVR8 and its photocycle regulators.
文摘Plants have evolved and perfected a series of light receptors to feel the light at different bands and regulate the expression, modification and interaction of related genes in plants through signal transduction. So far, many photoreceptors have been identified in plants, UVR8 has recently been identified as a receptor for UV-B light. This paper cloned a WD40 gene related to UVR8 protein subunit, named RrRUP2, based on the Rosa rugose transcriptome data, using Rosa rugose “Zi zhi” as experimental materials. The full length of cDNA of the gene was obtained by RT-PCR and RACE methods. The total length of this gene is 1173 bp, and it encodes 390 amino acids. After bioinformatics analysis, the molecular formula C3415H5659N1173O1434S313 was predicted;the relative molecular weight was 96129.27 Da;the theoretical isoelectric point PI value was 5.00;and its instability index was 47.06. The total average hydrophobic index was 0.750. In the secondary structure of RrRUP2 protein, there are 10 α-helix, 45 β-helix, 181 Random coil, and 154 Extended strand. Gene Bank Blast results showed that the amino acid sequence encoded by RrRUP2 was more than 90% homologous with the RUP2 protein of Rosa chinensis, Fragaria, Malus, Pyrus, Prunus, Juglans, Arabidopsis and Tobacco, so it can be inferred that the RrRUP2 gene is a WD repeat-containing protein. Regarding to fluorescence quantitative expression analysis of RrRUP2, we find its experssion pattern is corresponded with the accumulation of anthocyanins.
基金supported by the National Natural Science Foundation of China(Nos.52371222 and 52271211)the Natural Science Foundation of Hunan Province in China(Nos.2025JJ60350,2024JJ4022,and 2023JJ30277)+1 种基金the Key Research and Development Program of Hunan Province(No.2023GK2035)HORIZON–Marie Sk?odowska–Curie Actions–2021–PF(No.101065098),European Union
文摘Developing efficient and stable catalysts for the hydrogen evolution reaction(HER)is essential for advancing anion-exchange membrane water electrolyzer(AEMWE)technology.In this study,we present a facile microwave reduction and low-temperature phosphorization strategy to synthesize a highly efficient HER catalyst,comprising P,N-codoped carbon-supported RuP_(2)nanocluster(RuP_(2)@PNC).RuP_(2)@PNC demonstrates outstanding HER performance,achieving overpotentials of 18 and 44 mV at a current density of 10 mA cm^(-2)in alkaline and acidic media,respectively.Furthermore,an AEMWE device utilizing RuP_(2)@PNC as the cathode catalyst delivers a current density of 0.5 A cm^(-2)at a cell voltage of 1.84 V and exhibits remarkable stability over 150 h of operation.Experimental analyses and density functional theory(DFT)calculations reveal that the synergistic effects of P,N-codoped and the unique structure of RuP_(2)enhance electron transfer between Ru and the support,optimize the electronic structure,and regulate the d–band center of Ru.These features improve water adsorption,weaken the Ru–H binding strength,and facilitate efficient H_(2)desorption,collectively driving the superior HER activity of RuP_(2)@PNC.This work offers an effective design strategy for high-performance HER catalysts and provides valuable insights for accelerating the development of AEMWE technology.
