The consensus motif for N-myristoylation of plant proteins in a wheat germ cell-free translation system

The induction of rat liver zinc-thioneins mRNA was studied in a wheat germ cell-free translation system. Liver poly A rich polysomal RNA was isolated from rats which had been injected with zinc sulfate 5 h previously. These RNA preparations stimulated the incorporation of [35S]cystine into trichloroacetic acid insoluble proteins when assayed in the cell-free synthetic system. The translation products were characterized by Sephadex G-75 chromatography in 8 M urea – 50 mM β-mercaptoethanol, by disc gel electrophoresis in 4 M urea – Tris–glycine buffer (pH 9.2), and by peptide fingerprinting with pepsin. These results were identical with authentic rat liver zinc-thioneins. The zinc-thioneins mRNA activity in the control rats, however, was minimal. The stimulation in zinc-thioneins synthesis observed in the cell-free synthesis was similar to the increased synthesis of these polypeptides in vivo.

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Production of yeast tRNA (m7G46) methyltransferase (Trm8–Trm82 complex) in a wheat germ cell-free translation system

Journal of Biotechnology ◽

10.1016/j.jbiotec.2007.11.009 ◽

2008 ◽

Vol 133 (4) ◽

pp. 453-460 ◽

Cited By ~ 11

Author(s):

Keisuke Matsumoto ◽

Chie Tomikawa ◽

Takashi Toyooka ◽

Anna Ochi ◽

Yoshitaka Takano ◽

...

Keyword(s):

Germ Cell ◽

Wheat Germ ◽

Translation System ◽

Yeast Trna ◽

Free Translation

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Hetero subunit interaction and RNA recognition of yeast tRNA (m7G46) methyltransferase synthesized in a wheat germ cell-free translation system

Nucleic Acids Symposium Series ◽

10.1093/nass/nrm180 ◽

2007 ◽

Vol 51 (1) ◽

pp. 359-360 ◽

Cited By ~ 1

Author(s):

Y. Muneyoshi ◽

K. Matsumoto ◽

C. Tomikawa ◽

T. Toyooka ◽

A. Ochi ◽

...

Keyword(s):

Germ Cell ◽

Wheat Germ ◽

Translation System ◽

Rna Recognition ◽

Subunit Interaction ◽

Yeast Trna ◽

Free Translation

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Gene expression in Acetabularia. I. Calibration of wheat germ cell-free translation system proteins as internal references for two-dimensional electrophoresis

Journal of Cell Science ◽

10.1242/jcs.58.1.23 ◽

1982 ◽

Vol 58 (1) ◽

pp. 23-33

Author(s):

R.L. Shoeman ◽

H.G. Schweiger

Keyword(s):

Germ Cell ◽

Isoelectric Point ◽

Wheat Germ ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

In Vitro Translation ◽

Translation System ◽

Two Dimensional ◽

Free Translation

Modification of existing two-dimensional techniques enables isoelectric focusing and sodium dodecyl sulphate polyacrylamide gel electrophoresis of complex mixtures of proteins to be completed within 8 h. The method was optimized to separate the protein components of a wheat germ cell-free translation system, providing a statistically proven resolution better than 0. 03 of a pH unit for the isoelectric point and 1000 for Mr. Fourteen of the more than 300 proteins separated were characterized with respect to Mr and isoelectric point relative to standard proteins under the same conditions. Stained wheat germ proteins thus serve as internal standards for analysis of in vitro translation products.

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