Enhanced expression of a nuclease gene in leaves of barley plants under salt stress

Muramoto, Yasunori; Watanabe, Akira; Nakamura, Toshihide; Takabe, Tetsuko

doi:10.1016/s0378-1119(99)00193-6

Cited by 63 publications

(31 citation statements)

References 18 publications

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“…In such cases, the presence of the gene can be inferred through experimental assays for acid nuclease activity, although the potential for false positives is quite high. To date, assays for acid nuclease activity have given positive results in a fungus Cordyceps (Ye et al (2003)), the angiosperm plant Hordeum (Muramoto et al, 1999), and in Euglena, a basal protist (Ikeda and Takata, 2002). However, in some of these cases, such as in Hordeum, the nuclease activity is Zinc-mediated and consequently almost certainly not due to DNase II.…”

Section: Introductionmentioning

confidence: 99%

The phylogeny and evolution of deoxyribonuclease II: An enzyme essential for lysosomal DNA degradation

Shpak

Kugelman

Varela-Ramı́rez

et al. 2008

Molecular Phylogenetics and Evolution

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Deoxyribonuclease II (DNase II) is an endonuclease with optimal activity at low pH, localized within the lysosomes of higher eukaryotes. The origin of this enzyme remains in dispute, and its phylogenetic distribution leaves many questions about its subsequent evolutionary history open. Earlier studies have documented its presence in various metazoans, as well as in Dictyostelium, Trichomonas and, anomalously, a single genus of bacteria (Burkholderia). This study makes use of searches of the genomes of various organisms against known DNase II query sequences, in order to determine the likely point of origin of this enzyme among cellular life forms. Its complete absence from any other bacteria makes prokaryotic origin unlikely. Convincing evidence exists for DNase II homologs in Alveolates such as Paramecium, Heterokonts such as diatoms and water molds, and even tentative matches in green algae. Apparent absences include red algae, plants, fungi, and a number of parasitic organisms. Based on this phylogenetic distribution and hypotheses of eukaryotic relationships, the most probable explanation is that DNase II has been subject to multiple losses. The point of origin is debatable, though its presence in Trichomonas and perhaps in other evolutionarily basal "Excavate" protists such as Reclinomonas, strongly support the hypothesis that DNase II arose as a plesiomorphic trait in eukaryotes. It probably evolved together with phagocytosis, specifically to facilitate DNA degradation and bacteriotrophy. The various absences in many eukaryotic lineages are accounted for by loss of phagotrophic function in intracellular parasites, in obligate autotrophs, and in saprophytes.

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Section: Introductionmentioning

confidence: 99%

The phylogeny and evolution of deoxyribonuclease II: An enzyme essential for lysosomal DNA degradation

Shpak

Kugelman

Varela-Ramı́rez

et al. 2008

Molecular Phylogenetics and Evolution

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“…34) In our study, the transcript of SoPR10 was induced by nitrate and NaCl treatment, which meant that it might play important roles under salt stress. Earlier studies reported that PR-10 expression changed in response to drought stress in pine, 35) barley, 36) and birch. 37) After drought stress treatment, BetvIAFP showed the highest expression after 1 h and gradually decreased from 1 to 24 h treatments.…”

Section: The Expression Of Sopr10 Under Other Abiotic Stressesmentioning

confidence: 94%

Molecular cloning and characterization of pathogenesis-related protein family 10 gene from spinach (SoPR10)

Bai

Long

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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PR10 genes encode small, intracellular proteins that respond to biotic and abiotic stresses. In this study, a cDNA clone (designated as SoPR10, GenBank Accession No. KC142174) encoding a PR10 protein from spinach (Spinacia oleracea L.) was isolated and characterized. SoPR10 encoded a 161-amino acid polypeptide with a predicted molecular mass of 19.76 kDa and a pI of 4.61. Real-time quantitative analysis indicated that SoPR10 was constitutively expressed in root and shoot. The abundance of SoPR10 in salt-resistant cultivar (Chaoji) was generally greater than in salt-sensitive cultivar (Daye) under 160 mM L−1 treatment for 0.5, 3, and 6 h. The expression of SoPR10 was also induced by other abiotic stresses including polyethylene glycol, NaCl, salicylic acid, and H2O2. Our results indicated that SoPR10 might play important roles under nitrate stress and other abiotic stresses.

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“…The isolation and characterization of cDNAs encoding two S1-type DNases (BEN1 and ZEN1) that can be involved in the PCD of plants have been described [1]. Furthermore, Zn 2+ -dependent endonuclease cDNAs (Bnuc1) isolated from salt-stressed or senescent leaves in barley were detected [20]. The S1-type and Zn 2+ -dependent DNase groups have been associated with PCD [1,27,36].…”

Section: Introductionmentioning

confidence: 99%

Localization of BEN1-LIKE protein and nuclear degradation during development of metaphloem sieve elements inTriticum aestivumL.

Cai¹,

Zhang²,

Zhou³

et al. 2015

Acta Biologica Hungarica

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Metaphloem sieve elements (MSEs) in the developing caryopsis of Triticum aestivum L. undergo a unique type of programmed cell death (PCD); cell organelles gradually degrade with the MSE differentiation while mature sieve elements keep active. This study focuses on locating BEN1-LIKE protein and nuclear degradation in differentiating MSEs of wheat. Transmission electron microscopy (TEM) showed that nuclei degraded in MSE development. First, the degradation started at 2-3 days after flowering (DAF). The degraded fragments were then swallowed by phagocytic vacuoles at 4 DAF. Finally, nuclei almost completely degraded at 5 DAF. We measured the BEN1-LIKE protein expression in differentiating MSEs. In situ hybridization showed that BEN1-LIKE mRNA was a more obvious hybridization signal at 3-4 DAF at the microscopic level. Immuno-electron microscopy further revealed that BEN1-LIKE protein was mainly localized in MSE nuclei. Furthermore, MSE differentiation was tested using a TSQ Zn 2+ fluorescence probe which showed that the dynamic change of Zn 2+ accumulation was similar to BEN1-LIKE protein expression. These results suggest that nucleus degradation in wheat MSEs is associated with BEN1-LIKE protein and that the expression of this protein may be regulated by Zn 2+ accumulation variation.

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Enhanced expression of a nuclease gene in leaves of barley plants under salt stress

Cited by 63 publications

References 18 publications

The phylogeny and evolution of deoxyribonuclease II: An enzyme essential for lysosomal DNA degradation

The phylogeny and evolution of deoxyribonuclease II: An enzyme essential for lysosomal DNA degradation

Molecular cloning and characterization of pathogenesis-related protein family 10 gene from spinach (SoPR10)

Localization of BEN1-LIKE protein and nuclear degradation during development of metaphloem sieve elements inTriticum aestivumL.

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