Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena. / Andreasen, P H; Dreisig, H; Kristiansen, K.

In: Biochemical Journal, Vol. 244, No. 2, 1987, p. 331-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Andreasen, PH, Dreisig, H & Kristiansen, K 1987, 'Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena', Biochemical Journal, vol. 244, no. 2, pp. 331-5. <http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1147995>

APA

Andreasen, P. H., Dreisig, H., & Kristiansen, K. (1987). Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena. Biochemical Journal, 244(2), 331-5. http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1147995

Vancouver

Andreasen PH, Dreisig H, Kristiansen K. Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena. Biochemical Journal. 1987;244(2):331-5.

Author

Andreasen, P H ; Dreisig, H ; Kristiansen, K. / Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena. In: Biochemical Journal. 1987 ; Vol. 244, No. 2. pp. 331-5.

Bibtex

@article{859604e013c511de8478000ea68e967b,
title = "Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena",
abstract = "The codon usage of Tetrahymena thermophila and other ciliates deviates from the 'universal genetic code' in that UAA and probably UAG are not translational termination signals but code for glutamine. Therefore, translation in vitro of mRNA from Tetrahymena in a reticulocyte lysate is prematurely terminated if a UAA or UAG triplet is present in the reading frame of the mRNA. We show that the addition of a subcellular fraction from Tetrahymena thermophila enables a rabbit reticulocyte lysate to translate Tetrahymena mRNAs into full-sized proteins. The activity of the subcellular fraction is shown to depend on the combined function of a protein component(s) and a tRNA(s). The subcellular fraction is easily prepared and its usefulness for the identification of isolated mRNAs from Tetrahymena by their translation products in vitro is demonstrated.",
author = "Andreasen, {P H} and H Dreisig and K Kristiansen",
note = "Keywords: Animals; Codon; Electrophoresis, Polyacrylamide Gel; Protein Biosynthesis; Proteins; RNA, Messenger; Rabbits; Reticulocytes; Subcellular Fractions; Tetrahymena",
year = "1987",
language = "English",
volume = "244",
pages = "331--5",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Unusual ciliate-specific codons in Tetrahymena mRNAs are translated correctly in a rabbit reticulocyte lysate supplemented with a subcellular fraction from Tetrahymena

AU - Andreasen, P H

AU - Dreisig, H

AU - Kristiansen, K

N1 - Keywords: Animals; Codon; Electrophoresis, Polyacrylamide Gel; Protein Biosynthesis; Proteins; RNA, Messenger; Rabbits; Reticulocytes; Subcellular Fractions; Tetrahymena

PY - 1987

Y1 - 1987

N2 - The codon usage of Tetrahymena thermophila and other ciliates deviates from the 'universal genetic code' in that UAA and probably UAG are not translational termination signals but code for glutamine. Therefore, translation in vitro of mRNA from Tetrahymena in a reticulocyte lysate is prematurely terminated if a UAA or UAG triplet is present in the reading frame of the mRNA. We show that the addition of a subcellular fraction from Tetrahymena thermophila enables a rabbit reticulocyte lysate to translate Tetrahymena mRNAs into full-sized proteins. The activity of the subcellular fraction is shown to depend on the combined function of a protein component(s) and a tRNA(s). The subcellular fraction is easily prepared and its usefulness for the identification of isolated mRNAs from Tetrahymena by their translation products in vitro is demonstrated.

AB - The codon usage of Tetrahymena thermophila and other ciliates deviates from the 'universal genetic code' in that UAA and probably UAG are not translational termination signals but code for glutamine. Therefore, translation in vitro of mRNA from Tetrahymena in a reticulocyte lysate is prematurely terminated if a UAA or UAG triplet is present in the reading frame of the mRNA. We show that the addition of a subcellular fraction from Tetrahymena thermophila enables a rabbit reticulocyte lysate to translate Tetrahymena mRNAs into full-sized proteins. The activity of the subcellular fraction is shown to depend on the combined function of a protein component(s) and a tRNA(s). The subcellular fraction is easily prepared and its usefulness for the identification of isolated mRNAs from Tetrahymena by their translation products in vitro is demonstrated.

M3 - Journal article

C2 - 3663125

VL - 244

SP - 331

EP - 335

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

ID: 11368414