Effects of Fe<sup>3+</sup>and Zn<sup>2+</sup>on the Structural and Thermodynamic Properties of a Soybean ASR Protein

Li, Ranhui; Liu, Guobao; Wang, Hui; Zheng, Youliang

doi:10.1271/bbb.120666

Cited by 31 publications

(43 citation statements)

References 26 publications

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“…Moreover, rice ASR1 can scavenge ROS, 50 whereas soybean ASR1 buffers metal ions and thus provides antioxidant protection. 51 Therefore, ASR1 is probably involved in ROS depuration through several different mechanisms. Regarding other stress-related pathways, significant reductions in proline contents have been described in Asr1-overexpressing tobacco leaves under salt stress.…”

Section: Metabolic Pathways Involved In Asr1 Stress Responsesmentioning

confidence: 99%

ASR1 transcription factor and its role in metabolism

Domínguez

Carrari

2015

Plant Signaling & Behavior

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Section: Metabolic Pathways Involved In Asr1 Stress Responsesmentioning

confidence: 99%

ASR1 transcription factor and its role in metabolism

Domínguez

Carrari

2015

Plant Signaling & Behavior

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“…Fluorescence studies of GmASR demonstrated three Fe 3+ binding sites and two Zn 2+ binding sites. Interestingly, GmASR is natively disordered in aqueous solution and remains disordered in the Fe 3+ -bound state [47]. In contrast, the natively disordered tomato ASR1 protein undergoes a transition to an ordered structure upon Zn 2+ binding.…”

Section: Circular Dichroism Analysismentioning

confidence: 99%

“…Therefore, resistance to proteolysis has been used as a tool to assess protein folding [26,47]. rAhSOD digestion pattern in the absence and presence of Cu 2+ or Zn 2+ revealed that in the presence of ions, rAhSOD proteolysis was highly limited (Fig.…”

Section: Limited Proteolysis By Metalsmentioning

confidence: 99%

“…Fluorescence intensity decreased when Cu 2+ , Zn 2+ , or Ni 2+ were added to protein suspension. Similarly, the addition [47].…”

Section: Limited Proteolysis By Metalsmentioning

confidence: 99%

“…AhSOD showed negligible secondary structure content-1.48 % for α-helix and 7.26 % for β-sheet, and the addition of Cu 2+ and Zn 2+ did not result in an increase of α-helix nor β-sheet structures in AhSOD. The absence of regular secondary structure also suggested that rAhSOD might be an IDP or a Bnatively disordered enzyme.^Similarly, GmASR is disordered in aqueous solution showing a single minimum at 198 nm in the CD spectrum that does not changed when Fe 3+ is added [47]. Also, the binding of Zn 2+ in Cor47 and Lti29 dehydrins (from Arabidopsis thaliana) has minor effects on CD spectra, thus suggesting that dehydrins maintain disordered structures even in the presence of metal ions [48].…”

Section: Circular Dichroism Analysismentioning

confidence: 99%

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Biochemical and Molecular Characterization of a Novel Cu/Zn Superoxide Dismutase from Amaranthus hypochondriacus L.: an Intrinsically Disordered Protein

Montero-Morán

Sampedro

Saab‐Rincón³

et al. 2015

Appl Biochem Biotechnol

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A novel Cu/ZnSOD from Amaranthus hypochondriacus was cloned, expressed, and characterized. Nucleotide sequence analysis showed an open reading frame (ORF) of 456 bp, which was predicted to encode a 15.6-kDa molecular weight protein with a pI of 5.4. Structural analysis showed highly conserved amino acid residues involved in Cu/Zn binding. Recombinant amaranth superoxide dismutase (rAhSOD) displayed more than 50 % of catalytic activity after incubation at 100 °C for 30 min. In silico analysis of Amaranthus hypochondriacus SOD (AhSOD) amino acid sequence for globularity and disorder suggested that this protein is mainly disordered; this was confirmed by circular dichroism, which showed the lack of secondary structure. Intrinsic fluorescence studies showed that rAhSOD undergoes conformational changes in two steps by the presence of Cu/Zn, which indicates the presence of two binding sites displaying different affinities for metals ions. Our results show that AhSOD could be classified as an intrinsically disordered protein (IDP) that is folded when metals are bound and with high thermal stability.

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Expression patterns of the ZmASR family during simulated drought stress in maize

Zhang

Guo

et al. 2021

Agronomy Journal

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Maize (Zea mays L.) is an important food crop. Maize production is adversely affected by abiotic stress, especially drought stress. The screening and characterization of the roles of stress-related genes in maize are thus essential for improving abiotic stress resistance. Abscisic acid-stress-ripening (ASR)-induced proteins with abscisic acid/water deficit stress (ABA/WDS) domains are a class of plant-specific transcription factors that play an important role in plant development, growth, and abiotic stress responses. In this study, nine members of the ASR-induced protein in maize (ZmASR) family were predicted and analyzed in maize in terms of gene structure, subcellular localization, amino acid sequence, physical and chemical properties, secondary structure, tertiary structure, and phosphorylation modification sites by bioinformatics. Analysis of regulatory promoter elements was performed to provide additional information about their distinctive tissue-specific expression and possible functions. To further investigate the function of these proteins in maize, the expression levels of ZmASRs in different tissues and in response to different drought stress treatments were analyzed using quantitative real-time polymerase chain reaction (qRT-PCR). The results showed that the nine members of the maize ZmASR family have very different expression levels in different organs and under different degrees of drought stress. Moreover, the expression levels of the nine members in the same organ also varied greatly with leaf age. These findings provide a reference for functional research of the maize ZmASR gene family. Our findings have important theoretical and practical significance for cultivating new drought-resistant maize varieties and promoting the development of the maize industry.

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Effects of Fe³⁺and Zn²⁺on the Structural and Thermodynamic Properties of a Soybean ASR Protein

Cited by 31 publications

References 26 publications

ASR1 transcription factor and its role in metabolism

ASR1 transcription factor and its role in metabolism

Biochemical and Molecular Characterization of a Novel Cu/Zn Superoxide Dismutase from Amaranthus hypochondriacus L.: an Intrinsically Disordered Protein

Expression patterns of the ZmASR family during simulated drought stress in maize

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Effects of Fe3+and Zn2+on the Structural and Thermodynamic Properties of a Soybean ASR Protein

Cited by 31 publications

References 26 publications

ASR1 transcription factor and its role in metabolism

ASR1 transcription factor and its role in metabolism

Biochemical and Molecular Characterization of a Novel Cu/Zn Superoxide Dismutase from Amaranthus hypochondriacus L.: an Intrinsically Disordered Protein

Expression patterns of the ZmASR family during simulated drought stress in maize

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Effects of Fe³⁺and Zn²⁺on the Structural and Thermodynamic Properties of a Soybean ASR Protein