Results 151 to 160 of about 5,387 (170)
Purification of transfer-RNA-nucleotidyltransferase from E. Coli B
Abstract Transfer-RNA-nucleotidyltransferase has been purified 1400-fold from E. coli B by liquid polymer phase fractionation and chromatography on DEAE-cellulose, hydroxylapatite, and QAE-Sephadex. The final preparation contains no detectable RNase I, RNase II, polynucleotide phosphorylase, ATPase, CTPase, or any of the aminoacyl-tRNA ...
Jon P. Miller, Georg R. Philipps
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Ribonucleases, ?RNA Nucleotidyltransferase, and the 3' Processing of ?RNA
Publisher Summary This chapter describes 3’ maturation and repair, with particular emphasis on the ribonucleases and tRNA nucleotidyltransferase, the enzymes that participate in these processes. All tRNA molecules are synthesized initially as tRNA precursors containing additional residues at their 5’ and 3‘ termini that must be removed to generate ...
Murray P. Deutscher
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Abstract Purified preparations of avian RNA tumor viruses contain a nucleotidyltransferase which catalyzes the addition of adenosine monophosphate and cytosine monophosphate at the 3′-end of certain transfer RNAs, probably in the sequence pCpCpAoh.
Anthony J. Faras +3 more
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t-RNA-nucleotidyltransferase activity in Lupinus luteus seeds
Abstract t -RNA-nucleotidyltransferase activity was detected in Lupinus luteus seed.The enzyme was partly purified, and some of its properties are described.
Henryk Cudny +2 more
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The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases
ATP- and NAD(+)-dependent DNA ligases, ATP-dependent RNA ligases and GTP-dependent mRNA capping enzymes comprise a superfamily of proteins that catalyze nucleotidyl transfer to polynucleotide 5' ends via covalent enzyme-(lysyl-N)-NMP intermediates. The superfamily is defined by five peptide motifs that line the nucleotide-binding pocket and contribute ...
Stewart Shuman, Christopher D. Lima
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Inhibition of RNA nucleotidyltransferase by 6-azauridine triphosphate
I. Goldberg, Murray Rabinowitz
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Transfer RNA metabolism in Escherichia coli cells deficient in tRNA nucleotidyltransferase
We have investigated the role of tRNA nucleotidyltransferase in transfer RNA metabolism using mutants ( cca mutants) of Escherichia coli deficient in this enzyme. Extracts of the most defective strain contained cca mutation into a variety of genetic backgrounds. However, tRNA from stationary phase cells was somewhat more defective.
Murray P. Deutscher +2 more
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tRNA Nucleotidyltransferase and The -C-C-A Terminus of Transfer RNA
Murray P. Deutscher
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Hans Klenow, Sune Frederiksen
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Richard J Maraia
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