ArticlePlant physiology2006
Cold-active winter rye glucanases with ice-binding capacity.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 71 citations in OpenAlex.
- Frost Tolerance Under Cold Flooding Involves the Presence of Specific PR Proteins and Is Linked to Snow Mould Pathogen Resistance.International journal of molecular sciences · 2026Article
- Involvement of Pathogenesis-Related Proteins and Their Roles in Abiotic Stress Responses in Plants.Biomolecules · 2025Review
- Genome-Wide Identification, Expression and Interaction Analysis ofCurrent issues in molecular biology · 2024Article
- Emerging Roles of β-Glucanases in Plant Development and Adaptative Responses.Plants (Basel, Switzerland) · 2022Review
- Basic β-1,3-Glucanase fromPlants (Basel, Switzerland) · 2021Article
- Repair of sub-lethal freezing damage in leaves of Arabidopsis thaliana.BMC plant biology · 2020Article
- Boreal pollen contain ice-nucleating as well as ice-binding 'antifreeze' polysaccharides.Scientific reports · 2017Article
- Ice-Binding Proteins in Plants.Frontiers in plant science · 2017Review
- β-1,3-1,4-glucanase gene from Bacillus velezensis ZJ20 exerts antifungal effect on plant pathogenic fungi.World journal of microbiology & biotechnology · 2016Article
- Identification of low temperature stress regulated transcript sequences and gene families in Italian cypress.Molecular biotechnology · 2015Article
- Antifreeze proteins enable plants to survive in freezing conditions.Journal of biosciences · 2014Review
- Antivirulence properties of an antifreeze protein.Cell reports · 2014Article
- Psychrotolerant antifungal Streptomyces isolated from Tawang, India and the shift in chitinase gene family.Extremophiles : life under extreme conditions · 2013Article
- Review
- Molecular analysis of the gene encoding a new chitinase from the marine psychrophilic bacterium Moritella marina and biochemical characterization of the recombinant enzyme.Extremophiles : life under extreme conditions · 2008Article
- Co-Localization of beta-1,3-Glucanases and Callose During Somatic Embryogenesis in Cichorium.Plant signaling & behavior · 2007Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extracellular pathogenesis-related proteins, including glucanases, are expressed at cold temperatures in winter rye (Secale cereale) and display antifreeze activity. We have characterized recombinant cold-induced glucanases from winter rye to further examine their roles and contributions to cold tolerance. Both basic beta-1,3-glucanases and an acidic beta-1,3;1,4-glucanase were expressed in Escherichia coli, purified, and assayed for their hydrolytic and antifreeze activities in vitro. All were found to be cold active and to retain partial hydrolytic activity at subzero temperatures (e.g. 14%-35% at -4 degrees C). The two types of glucanases had antifreeze activity as measured by their ability to modify the growth of ice crystals. Structural models for the winter rye beta-1,3-glucanases were developed on which putative ice-binding surfaces (IBSs) were identified. Residues on the putative IBSs were charge conserved for each of the expressed glucanases, with the exception of one beta-1,3-glucanase recovered from nonacclimated winter rye in which a charged amino acid was present on the putative IBS. This protein also had a reduced antifreeze activity relative to the other expressed glucanases. These results support the hypothesis that winter rye glucanases have evolved to inhibit the formation of large, potentially fatal ice crystals, in addition to having enzymatic activity with a potential role in resisting infection by psychrophilic pathogens. Glucanases of winter rye provide an interesting example of protein evolution and adaptation aimed to combat cold and freezing conditions.
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