Open AccessPhosphorolysis of Aminoacyl‐tRNA by Polynucleotide Phosphorylase from Escherichia coli
Author(s) -
Kaufmann G.,
Littauer U. Z.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00824.x
Subject(s) - phosphorolysis , polynucleotide phosphorylase , polynucleotide , pyrophosphate , purine nucleoside phosphorylase , biochemistry , transfer rna , escherichia coli , chemistry , stilbestrol , biology , enzyme , rna , diethylstilbestrol , purine , gene , hormone
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.