Subcellular distribution and functional properties of different forms of elongation factor EF1 from wheat embryos

Lanzani, G.A.; Caldiroli, E.; Zocchi, Graziano; Manzocchi, Lucia A.; Bollini, Roberto; Alberti, L. De

doi:10.1016/0005-2787(75)90298-1

Cited by 10 publications

(2 citation statements)

References 22 publications

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“…The molecular mass of the active peptide determined by SDS/PAGE was slightly higher (20 kDa) than that determined by gel-filtration (1 8 kDa). The inability to retain the capacity to bind GTP after denaturation with SDS shown by the 52-kDa protein agrees with its previous identification as the active form (EF-1 cx) of the elongation factor 1 (Lanzani et al, 1975;Sacchi et al, 1984).…”

Section: Discussionsupporting

confidence: 88%

“…The activity present in the L fraction (maximum at 52 ma) corresponds to the eukaryotic protein-synthesis elongation factor 1 (EF-lu) as reported previously in wheat seeds by Lanzani et al (1975) and Sacchi et al (1984). The GTP-binding activity present in the SL fraction, with a maximum at 18 kDa, does not correspond in molecular mass to any currently characterized cytosolic GTP-binding protein in higher plants.…”

Section: Binding Of [A-supporting

confidence: 62%

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A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

Saccht¹,

Pirovano²,

Lucchini³

et al. 1996

European Journal of Biochemistry

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A low-molecular-mass protein able to bind GTP in both native and SDS-denaturating conditions was detected in the cytosol of embryos from wheat (Triticum aestivum L.) seeds germinated for 40 h. The protein fulfilled most of the distinguishing criteria common to eukaryotic small GTP-binding proteins. It retained the ability to bind GTP after SDSPAGE and nitrocellulose blotting. The protein eluted from Sephadex G-200 gel filtration with a V,lV,, value corresponding to a molecular mass of 18 kDa, whereas on SDS/PAGE the molecular mass was 20 kDa. The native protein, which showed an intrinsic GTPase activity highly sensitive to NaF, bound the guanine nucleotide with high specificity and with a relatively high affinity (K', =85 nM). The GTP-binding protein was not detectable in other subcellular fractions; in the microsomal fraction, two other peptides of low molecular mass (23.5 and 21.5 kDa) with GTP-binding activity were detected. These results indicate that in the cytosolic fraction of germinating wheat embryos there is a 20-kDa protein which is biochemically similar to the known small GTP-binding proteins that currently have been detected almost exclusively in the membrane fraction of plant material.

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Section: Discussionsupporting

confidence: 88%

Section: Binding Of [A-supporting

confidence: 62%

A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

Saccht¹,

Pirovano²,

Lucchini³

et al. 1996

European Journal of Biochemistry

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Messenger ribonucleoprotein particles in dry wheat and rye embryos

Peumans

Carlier

1977

Planta

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Extracts prepared from dry wheat (Triticum aestivum L.; var. Cama) and rye (Secale cereale L.; var. Celestijner) embryos exhibit relatively high endogenous messenger activities in an in vitro protein synthesizing system: up to 400 pmol leucine are incorporated per 50 μl reaction mixture; the messenger/ribosome ratio is estimated at about 0.03. Sucrose gradient analysis of the incubation mixture during cellfree protein synthesis shows a progressive in vitro polysome formation with the native endogenous mRNPs. The translation of these messengers, although dependent on initiation, follows linear kinetics. The native mRNP particles can be separated on sucrose gradients in 6 distinct size classes with sedimentation values varying from 25 S to 104 S. Their size is strongly reduced after deproteinization so that the naked mRNAs sediment in a range between 8 S and 35 S. The molecular weights of the proteins synthesized under direction of the native RNA particles range from 12,000 to 70,000 as estimated by polyacrylamide gel electrophoresis.

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The translational system from wheat embryos: Some properties of the polypeptides associated in EF1_H

Lanzani

Caldiroli

Manzocchi³

et al. 1976

FEBS Letters

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Subcellular distribution and functional properties of different forms of elongation factor EF1 from wheat embryos

Cited by 10 publications

References 22 publications

A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

Messenger ribonucleoprotein particles in dry wheat and rye embryos

The translational system from wheat embryos: Some properties of the polypeptides associated in EF1_H

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Subcellular distribution and functional properties of different forms of elongation factor EF1 from wheat embryos

Cited by 10 publications

References 22 publications

A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

A Low‐Molecular‐Mass GTP‐Binding Protein in the Cytosol of Germinated Wheat Embryos

Messenger ribonucleoprotein particles in dry wheat and rye embryos

The translational system from wheat embryos: Some properties of the polypeptides associated in EF1H

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Product

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The translational system from wheat embryos: Some properties of the polypeptides associated in EF1_H