Partial purification and characterization of two Nicotiana tabacum leaf ribonucleases

Jervis, L.

doi:10.1016/s0031-9422(00)91402-x

Cited by 20 publications

(7 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1). These results agree well with conclusions reported for glycophytes (Reddi 1966, Wyen et al 1971, Lantero and Klosterman 1973, Gray 1974, Jervis 1974, although incubation conditions vary considerably from one analysis to the other.…”

Section: Discussionsupporting

confidence: 92%

Effect of NaCl salinity in vivo and in vitro on ribonuclease activity in the halophyte Suaeda maritima

Rouxel¹,

Billard²,

Boucaud³

1987

Physiologia Plantarum

View full text Add to dashboard Cite

Ribonuclease (EC 2.7.7.17) activity in the obligate halophyte Suaeda maritima (L.) Dum. var. macrocarpa Moq. was studied in relation to salinity (increasing concentrations of NaCl) of incubation and growth media. In vitro, the addition of 50 to 400 mM NaCl did not affect ribonuclease activity. This result, which was also found for Phaseolus vulgaris, indicates that the hydrolase is insensitive to high saline concentrations. The subcellular distribution of RNase activity did not change significantly with the salinity of the medium or with the age of the plant. The microsomal ribonuclease activity expressed on a fresh weight basis represented in every case less than 6% of the total activity. After 23 days of culture, the absence of salt stimulated the activity of soluble ribonuclease in aerial parts of Suaeda; inversely, the capacity of the enzyme was lower under optimal saline conditions (130 mM NaCl). This was also evidenced by transfer of whole plants from a non‐saline to a saline medium. Such a saline shock caused a decrease followed by a stabilization of the capacity of ribonuclease from Suaeda. The influx of NaCl in the tissues lowered the activity of the hydrolase.

show abstract

Section: Discussionsupporting

confidence: 92%

Effect of NaCl salinity in vivo and in vitro on ribonuclease activity in the halophyte Suaeda maritima

Rouxel¹,

Billard²,

Boucaud³

1987

Physiologia Plantarum

View full text Add to dashboard Cite

show abstract

“…10 and the stronger activity observed in this area in poly-d(A-T) control gels. The four major ribonuclease isoenzymes were found to be charge isomers, as was expected from the determination of a single molecular weight for this enzyme in tobacco leaves [ 5,6] .…”

Section: Discussionsupporting

confidence: 66%

“…In the soluble protein fraction of tobacco leaves, at least four types of nuclease activity have been characterized on the basis of their substrate specificity [5,6]. Although cultured tobacco cells upon electrophoresis yielded four bands of RNase activity as detected by diffusion of low molecular weight RNA into the gel [4] , in our hands similar methods led to a poorly defined, remarkably complex pattern when applied to soluble proteins from tobacco leaves.…”

Section: Introductionmentioning

confidence: 84%

Polynucleotide‐acrylamide gel electrophoresis of soluble nucleases from tobacco leaves

Loon

1975

FEBS Letters

View full text Add to dashboard Cite

“…However, most such studies have been performed using rather crude or poorly purified preparations of these enzymes (Wilson 1982). Most known plant RNases have been isolated and purified from the endosperm and scutella of developing seeds (Wilson 1968(Wilson , 1973, the leaves of several plants (Wyen et al 1971 ;Lantero and Klosterman 1973;Jervis 1974;Chevrier and Sarhan 1980), cotyledons (Barker et al 1974;Jacobsen 1980), and roots and seedlings (Kado 1968;Hirai and Asahi 1975;Kroeker et al 1976;Beopoulos et al 1978). Even though many plant seeds have been shown to contain RNase activities, only a few enzymes have been isolated from dry seeds (Wilson 1982).…”

Section: Introductionmentioning

confidence: 99%

Cusativin, a new cytidine-specific ribonuclease accumulated in seeds of Cucumis sativus L.

Arias

Iglesias

et al. 1994

Planta

View full text Add to dashboard Cite

Dry seeds of Cucumis sativus L. were found to contain a heat-sensitive endoribonuclease of a novel type which we have named cusativin. It was purified to apparent electrophoretic homogeneity by chromatography through S-Sepharose Fast Flow, Sephadex G-75, CM-Sepharose, Superdex 75-FPLC (fast protein liquid chromatography) and Mono S-FPLC. It is a single unglycosylated polypeptide chain with an apparent molecular mass (M(r)) of 22900. Polyclonal anti-cusativin antibodies raised in rabbits only reacted with melonin, the translation inhibitor from Cucumis melo L. Functional, Western blot and enzyme-linked immunosorbent assay (ELISA) analyses indicated that cusativin is present in the coat and cotyledons of dry seeds, but not in embryonic axes. Cusativin is accumulated in maturing seeds. By contrast, after seed germination there is degradation of the cusativin present in cotyledons but not that present in the seed coat. The preference of cusativin for polynucleotide cleavage was poly(C) >> poly(A) acids, poly(U) and poly(G) being unaffected by cusativin. Under the denaturing conditions used for RNA sequencing, cusativin acted only on poly(C). Cusativin proved to be useful for RNA sequencing, in particular, complementing the data obtained with RNase CL3. Cusativin represents a new class of plant RNase and, as far as we are aware, is the first plant enzyme that shows cleavage specificity for cytidine under the denaturing conditions of RNA sequencing.

show abstract

Partial purification and characterization of two Nicotiana tabacum leaf ribonucleases

Cited by 20 publications

References 21 publications

Effect of NaCl salinity in vivo and in vitro on ribonuclease activity in the halophyte Suaeda maritima

Effect of NaCl salinity in vivo and in vitro on ribonuclease activity in the halophyte Suaeda maritima

Polynucleotide‐acrylamide gel electrophoresis of soluble nucleases from tobacco leaves

Cusativin, a new cytidine-specific ribonuclease accumulated in seeds of Cucumis sativus L.

Contact Info

Product

Resources

About