1970European Journal of BiochemistryOpen access

Phosphorolysis of Aminoacyl‐tRNA by Polynucleotide Phosphorylase from Escherichia coli

Gabriel Kaufmann, Uriel Z. Littauer

Open full text 15 citations

Abstract

Valyl‐transfer ribonucleic acid was degraded by polynucleotide phosphorylase from Escherichia coli in the presence of phosphate or arsenate. A compound that was identified as 2′(3′)‐O‐valyladenosine 5′‐pyrophosphate was isolated from the phosphorolytic digest of valyl‐tRNA while 2′(3′)‐O‐valyladenosine 5′‐monophosphate was isolated from the arsenolytic digest. It was concluded that valyl‐tRNA can be phosphorolyzed by polynucleotide phosphorylase. The rate of phosphorolysis of aminoacylated tRNA was lower than that of uncharged tRNA. N‐blocked derivatives of valyl‐tRNA and phenylalanyl‐tRNA were also phosphorolyzed by polynucleotide phosphorylase. Some possible uses of nucleoside diphosphates substituted in their sugar moiety are suggested.

Open-access reader

About this research paper

What this paper is about

Valyl‐transfer ribonucleic acid was degraded by polynucleotide phosphorylase from Escherichia coli in the presence of phosphate or arsenate. A compound that was identified as 2′(3′)‐O‐valyladenosine 5′‐pyrophosphate was isolated from the phosphorolytic digest of valyl‐tRNA while 2′(3′)‐O‐valyladenosine 5′‐monophosphate was isolated from the arsenolytic digest. It was concluded that valyl‐tRNA can be phosphorolyzed by polynucleotide phosphorylase. The rate of phosphorolysis of aminoacylated tRNA was lower than that of uncharged tRNA. N‐blocked derivatives of valyl‐tRNA and phenylalanyl‐tRNA were also phosphorolyzed by polynucleotide phosphorylase. Some possible uses of nucleoside diphosphates substituted in their sugar moiety are suggested.

Why it matters

OpenAlex reports 15 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Valyl‐transfer ribonucleic acid was degraded by polynucleotide phosphorylase from Escherichia coli in the presence of phosphate or arsenate. A compound that was identified as 2′(3′)‐O‐valyladenosine 5′‐pyrophosphate was isolated from the phosphorolytic digest of valyl‐tRNA while 2′(3′)‐O‐valyladenosine 5′‐monophosphate was isolated from the arsenolytic digest. It was concluded that valyl‐tRNA can be phosphorolyzed by polynucleotide phosphorylase. The rate of phosphorolysis of aminoacylated tRNA was lower than that of uncharged tRNA. N‐blocked derivatives of valyl‐tRNA and phenylalanyl‐tRNA were also phosphorolyzed by polynucleotide phosphorylase. Some possible uses of nucleoside diphosphates substituted in their sugar moiety are suggested.

Key concepts: Phosphorolysis, Polynucleotide phosphorylase, Polynucleotide, Pyrophosphate, Purine nucleoside phosphorylase, Biochemistry, Transfer RNA, Escherichia coli

Related papers

Back to paper searchBrowse research topicsOriginal source
Phosphorolysis of Aminoacyl‐tRNA by Polynucleotide Phosphorylase from Escherichia coli — Research Paper | ScholarLens