Nuclease I from suspension-cultured Nicotiana tabacum: Purification and properties of the extracellular enzyme

Oleson, Arland E.; Janski, Alvin M.; Fahrlander, Paul D.; Wiesner, Thomas A.

doi:10.1016/0003-9861(82)90207-7

Cited by 19 publications

(14 citation statements)

References 34 publications

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“…3), the properties ofthe tomato extracellular enzyme meet the criteria of a RNase I (EC 3.1.27.1) according to the classification of plant nucleolytic enzymes introduced by Wilson (30). So far, only nucleases hydrolyzing both DNA and RNA were identified as extracellular plant nucleolytic enzymes (7,20,29). Except an RNase I secreted by corn scutella (29,30), RNases I are known as typical intracellular activities; an enzyme of that type was shown to be located in the vacuoles of the tomato cells used in this study (2 and references therein, 3).…”

Section: Discussionmentioning

confidence: 99%

Induction of an Extracellular Ribonuclease in Cultured Tomato Cells upon Phosphate Starvation

Nürnberger¹,

Abel²,

Jost³

et al. 1990

Plant Physiol.

108

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Suspension-cultured cells of tomato (Lycopersicon esculentum) start to secrete an RNA-degrading enzyme activity during transition from logarithmic to stationary growth phase. Using affinity chromatography on agarose-5-(4-aminophenyl-phosphoryl) uridine 3'(2') monophosphate as a powerful and final enrichment step, the enzyme was purified to homogeneity and characterized as ribonuclease I (RNase I) according to the following data: (a) it has an Mr of 22,000 (sodium dodecyl sulfatepolyacrylamide gel electrophoresis), a pH-optimum of pH 5.5, a pi of 3.9, and its activity was found to be insensitive to EDTA; (b) the enzyme splits single-stranded RNA endonucleolytically by a phosphotransferase reaction yielding 2',3'-cNMPs as primary monomeric products; (c) as studied with diribonucleoside monophosphates as substrates, the enzyme exhibits a pronounced preference for 5' purine residues adjacent to the cleavage site.

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Section: Discussionmentioning

confidence: 99%

Induction of an Extracellular Ribonuclease in Cultured Tomato Cells upon Phosphate Starvation

Nürnberger¹,

Abel²,

Jost³

et al. 1990

Plant Physiol.

108

View full text Add to dashboard Cite

show abstract

“…Although nuclease I from Nicotiana tabacum is a monomer of 35 kDa, two forms of the enzyme with pI of 5.2 and 5.6 could be resolved by electrofocussing. These forms did not exhibit any signi¢cant di¡erence in their catalytic properties [117]. In contrast, acid and neutral nucleases from alfalfa seeds, although exhibiting di¡erent pH optima, had pI values in the acidic range (4.9 and 5.3, respectively) [118].…”

Section: Isoelectric Pointmentioning

confidence: 99%

“…These results also indicated that in a polymeric substrate, the bases adjacent to the most preferred base also in£uence the speci¢city of the enzyme. A study of the rates of hydrolysis of dinucleoside monophosphates by nuclease I from Nicotiana tabacum [117] revealed a strong preference for purine nucleosides as the 5P residue, with slight preference for uridine as the 3P residue. Similar observations were made with barley nuclease [94].…”

Section: Base/linkage Speci¢citymentioning

confidence: 99%

Single-strand-specific nucleases

Desai

2003

FEMS Microbiology Reviews

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Single-strand-specific nucleases are multifunctional enzymes and widespread in distribution. Their ability to act selectively on singlestranded nucleic acids and single-stranded regions in double-stranded nucleic acids has led to their extensive application as probes for the structural determination of nucleic acids. Intracellularly, they have been implicated in recombination, repair and replication, whereas extracellular enzymes have a role in nutrition. Although more than 30 single-strand-specific nucleases from various sources have been isolated till now, only a few enzymes (S1 nuclease from Aspergillus oryzae, P1 nuclease from Penicillium citrinum and nucleases from Alteromonas espejiana, Neurospora crassa, Ustilago maydis and mung bean) have been characterized to a significant extent. Recently, some of these enzymes have been cloned, their crystal structures solved and their interactions with different substrates have been established. The detection, purification, characteristics, structure^function correlations, biological role and applications of single-strand-specific nucleases are reviewed.

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“…Many examples of such activities have been reported. They include proteins with nuclease I characteristics from mung bean (Laskowski, 1980), tobacco cell suspension cultures (Oleson et al, 1982), tobacco pollen (Matousek and Tupy, 1984), barley Ho, 1986, 1987), zinnia (Zinnia elegans) (Thelen and Northcote, 1989), rye (Siwecka et al, 1989;el Adlouni et al, 1993), and Lentinula edodes (Kobayashi et al, 1995). In addition, a number of activities with some similarities to the tobacco pollen nuclease I (Matousek and Tupy, 1984) have been identified in pollen from various other plants (Matousek and Tupy, 1985).…”

mentioning

confidence: 99%

Identification of BFN1, a Bifunctional Nuclease Induced during Leaf and Stem Senescence in Arabidopsis

et al. 2000

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Nuclease I enzymes are responsible for the degradation of RNA and single-stranded DNA during several plant growth and developmental processes, including senescence. However, in the case of senescence the corresponding genes have not been reported. We describe the identification and characterization of BFN1 of Arabidopsis, and demonstrate that it is a senescence-associated nuclease I gene. BFN1 nuclease shows high similarity to the sequence of a barley nuclease induced during germination and a zinnia (Zinnia elegans) nuclease induced during xylogenesis. In transgenic plants overexpressing the BFN1 cDNA, a nuclease activity of about 38 kD was detected on both RNase and DNase activity gels. Levels of BFN1 mRNA were extremely low or undetectable in roots, leaves, and stems. In contrast, relatively high BFN1 mRNA levels were detected in flowers and during leaf and stem senescence. BFN1 nuclease activity was also induced during leaf and stem senescence. The strong response of the BFN1 gene to senescence indicated that it would be an excellent tool with which to study the mechanisms of senescence induction, as well as the role of the BFN1 enzyme in senescence using reverse genetic approaches in Arabidopsis.

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Nuclease I from suspension-cultured Nicotiana tabacum: Purification and properties of the extracellular enzyme

Cited by 19 publications

References 34 publications

Induction of an Extracellular Ribonuclease in Cultured Tomato Cells upon Phosphate Starvation

Induction of an Extracellular Ribonuclease in Cultured Tomato Cells upon Phosphate Starvation

Single-strand-specific nucleases

Identification of BFN1, a Bifunctional Nuclease Induced during Leaf and Stem Senescence in Arabidopsis

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