Amino acid acceptor activity of tRNA-C-C-C-A

Arthur H. Kirschenbaum; Murray P. Deutscher

doi:10.1016/0006-291X(76)91136-0

Amino acid acceptor activity of tRNA-C-C-C-A

Arthur H. Kirschenbaum, Murray P. Deutscher

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Rabbit liver tRNA nucleotidyltransferase was used to synthesize modified tRNA molecules containing an additional CMP residue at the 3′ terminus. In the first step tRNA-C-C was converted to tRNA-C-C-C by a minor activity of the purified enzyme. In the second step the lengthened molecules were converted to tRNA-C-C-C-A. AMP addition to tRNA-C-C-C occurred at about 50% the rate with tRNA-C-C. Aminoacylation studies indicated that tRNA-C-C-C-A was active for acceptance of at least 12 amino acids.

Original language	English (US)
Pages (from-to)	258-264
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	70
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(76)91136-0
State	Published - May 3 1976

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Rabbit liver tRNA nucleotidyltransferase was used to synthesize modified tRNA molecules containing an additional CMP residue at the 3′ terminus. In the first step tRNA-C-C was converted to tRNA-C-C-C by a minor activity of the purified enzyme. In the second step the lengthened molecules were converted to tRNA-C-C-C-A. AMP addition to tRNA-C-C-C occurred at about 50% the rate with tRNA-C-C. Aminoacylation studies indicated that tRNA-C-C-C-A was active for acceptance of at least 12 amino acids.",

author = "Kirschenbaum, {Arthur H.} and Deutscher, {Murray P.}",

year = "1976",

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AU - Kirschenbaum, Arthur H.

AU - Deutscher, Murray P.

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N2 - Rabbit liver tRNA nucleotidyltransferase was used to synthesize modified tRNA molecules containing an additional CMP residue at the 3′ terminus. In the first step tRNA-C-C was converted to tRNA-C-C-C by a minor activity of the purified enzyme. In the second step the lengthened molecules were converted to tRNA-C-C-C-A. AMP addition to tRNA-C-C-C occurred at about 50% the rate with tRNA-C-C. Aminoacylation studies indicated that tRNA-C-C-C-A was active for acceptance of at least 12 amino acids.

AB - Rabbit liver tRNA nucleotidyltransferase was used to synthesize modified tRNA molecules containing an additional CMP residue at the 3′ terminus. In the first step tRNA-C-C was converted to tRNA-C-C-C by a minor activity of the purified enzyme. In the second step the lengthened molecules were converted to tRNA-C-C-C-A. AMP addition to tRNA-C-C-C occurred at about 50% the rate with tRNA-C-C. Aminoacylation studies indicated that tRNA-C-C-C-A was active for acceptance of at least 12 amino acids.

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