ArticlePlant physiology2007
Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 100 citations in OpenAlex.
- The MaASR3-MaHDT1 module modulates high-temperature-inhibited chlorophyll breakdown in banana fruit by suppressing the E3 ligase MaNIP1.Horticulture research · 2025Article
- Genome-Wide Identification and Expression Profiling ofPlants (Basel, Switzerland) · 2025Article
- ASR gene family: a case of tandem-drive evolution.Frontiers in molecular biosciences · 2025Article
- Genome-Wide Identification of the PeanutInternational journal of molecular sciences · 2024Article
- Development History, Structure, and Function ofInternational journal of molecular sciences · 2024Review
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- Grape ASR Regulates Glucose Transport, Metabolism and Signaling.International journal of molecular sciences · 2022Article
- Grape ASR-Silencing Sways Nuclear Proteome, Histone Marks and Interplay of Intrinsically Disordered Proteins.International journal of molecular sciences · 2022Article
- Investigating Intrinsically Disordered Proteins With Brownian Dynamics.Frontiers in molecular biosciences · 2022Article
- Multiomics study of a heterotardigrade, Echinisicus testudo, suggests the possibility of convergent evolution of abundant heat-soluble proteins in Tardigrada.BMC genomics · 2021Article
- Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family.International journal of molecular sciences · 2021Article
- Characterization of ASR gene and its role in drought tolerance in chickpea (Cicer arietinum L.).PloS one · 2020Article
- Comprehensive Analysis of the Cadmium Tolerance of Abscisic Acid-, Stress- and Ripening-Induced Proteins (ASRs) in Maize.International journal of molecular sciences · 2019Article
- Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene.PloS one · 2018Article
- Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Scientific reports · 2017Article
- Article
- OsASR5 enhances drought tolerance through a stomatal closure pathway associated with ABA and HPlant biotechnology journal · 2017Article
- Proteomic Analysis of Differentially Accumulated Proteins in Cucumber (Frontiers in plant science · 2017Article
- Molecular cloning and characterization of drought stress responsive abscisic acid-stress-ripening (Asr 1) gene from wild jujube, Ziziphus nummularia (Burm.f.) Wight & Arn.Molecular biology reports · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Abscisic acid stress ripening 1 (ASR1) is a low molecular weight plant-specific protein encoded by an abiotic stress-regulated gene. Overexpression of ASR1 in transgenic plants increases their salt tolerance. The ASR1 protein possesses a zinc-dependent DNA-binding activity. The DNA-binding site was mapped to the central part of the polypeptide using truncated forms of the protein. Two additional zinc-binding sites were shown to be localized at the amino terminus of the polypeptide. ASR1 protein is presumed to be an intrinsically unstructured protein using a number of prediction algorithms. The degree of order of ASR1 was determined experimentally using nontagged recombinant protein expressed in Escherichia coli and purified to homogeneity. Purified ASR1 was shown to be unfolded using dynamic light scattering, gel filtration, microcalorimetry, circular dichroism, and Fourier transform infrared spectrometry. The protein was shown to be monomeric by analytical ultracentrifugation. Addition of zinc ions resulted in a global change in ASR1 structure from monomer to homodimer. Upon binding of zinc ions, the protein becomes ordered as shown by Fourier transform infrared spectrometry and microcalorimetry, concomitant with dimerization. Tomato (Solanum lycopersicum) leaf soluble ASR1 is unstructured in the absence of added zinc and gains structure upon binding of the metal ion. The effect of zinc binding on ASR1 folding and dimerization is discussed.
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