Open AccessMonofunctional Substrates of Polynucleotide Phosphorylase
Author(s) -
Kaufmann Gabriel,
Fridkin Matityahu,
Zutra Aliza,
Littauer Uriel Z.
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb19649.x
Subject(s) - polynucleotide phosphorylase , oligonucleotide , polynucleotide , residue (chemistry) , purine nucleoside phosphorylase , chemistry , escherichia coli , thymine , stereochemistry , oligonucleotide synthesis , biochemistry , nucleoside , enzyme , dna , purine , gene
Polynucleotide phosphorylase from Escherichia coli cells catalyzes the transfer of a single nucleotidyl residue from each of the 2′(3′)‐ O ‐isovalerylesters of ADP, GDP, CDP and UDP to the initiator oligonucleotide, A‐A‐A. The products of these reactions are identified as the 2′(3′)‐ O ‐isovaleryl esters of the corresponding tetranucleotides A‐A‐A‐A, A‐A‐A‐G, A‐A‐A‐C and A‐A‐A‐U. The 2′(3′)‐ O ‐isovaleryl residue can be removed from the product by treatment with aqueous methanolic ammonia under conditions that do not significantly damage the oligonucleotide chains. The monoaddition of 2′(3′)‐ O ‐acyl esters of nucleoside diphosphates to an oligonucleotide acceptor is proposed as a method for the stepwise synthesis of oligoribonucleotides of defined sequence.