Results 21 to 30 of about 5,387 (170)

The influence of spermidine on the reaction of RNA nucleotidyltransferase

open access: closedBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1968
Abstract 1. 1. RNA synthesis, catalyzed by RNA nucleotidyltransferase ( Escherichia coli B) and directed by native, double-stranded DNA, is significantly increased by spermidine. 2. 2. By use of doubly labeled ATP ([8- 14 C]- and [γ- 32 P]-) and by zone centrifugation, we could show that, in the presence of spermidine, more RNA chains are ...
Eiko E. Petersen, Hans Kröger, U. Hagen
  +7 more sources

Apparent non-involvement of transfer RNA nucleotidyltransferase in the biosynthesis of Escherichia coli suppressor transfer RNAs

open access: hybridJournal of Molecular Biology, 1975
Abstract Transfer RNA nucleotidyltransferase has previously been shown to be required for the normal growth of Escherichia coli and for the biosynthesis of some bacteriophage T4 tRNAs. In order to obtain information about the involvement of this enzyme in E.
Jeffrey W Morse, Murray P. Deutscher
openalex   +3 more sources

Recognition of the tRNA-like structure in tobacco mosaic viral RNA by ATP/CTP:tRNA nucleotidyltransferases from Escherichia coli and Saccharomyces cerevisiae.

open access: hybridJournal of Biological Chemistry, 1990
The 3'-terminal tRNA-like structure of the tobacco mosaic virus RNA interacts with ATP/CTP:tRNA nucleotidyltransferases from Escherichia coli or yeast in much the same manner as do tRNAs. Primary sites of interaction cluster near the 3' end and in the loop proposed to be analogous to the psi-loop of a tRNA.
Lisa A. Hegg   +2 more
openalex   +3 more sources

Transfer RNA pyrophosphorolysis with CTP(ATP):tRNA nucleotidyltransferase. A direct route to tRNAs modified at the 3' terminus.

open access: hybridJournal of Biological Chemistry, 1983
The pyrophosphorolysis of tRNA by yeast CTP-(ATP):tRNA nucleotidyltransferase has been studied in an effort to define the behavior of the enzyme and the experimental parameters that lead to net loss of the 3'-terminal nucleotide or to nucleotide exchange.
Terry Francis   +3 more
openalex   +3 more sources

The Battle for Survival: The Role of RNA Non-Canonical Tails in the Virus–Host Interaction

open access: yesMetabolites, 2023
Terminal nucleotidyltransferases (TENTs) could generate a ‘mixed tail’ or ‘U-rich tail’ consisting of different nucleotides at the 3′ end of RNA by non-templated nucleotide addition to protect or degrade cellular messenger RNA.
Xianghui Wen, Ahsan Irshad, Hua Jin
doaj   +1 more source

Promiscuous splicing-derived hairpins are dominant substrates of tailing-mediated defense of miRNA biogenesis in mammals

open access: yesCell Reports, 2023
Summary: Canonical microRNA (miRNA) hairpins are processed by the RNase III enzymes Drosha and Dicer into ∼22 nt RNAs loaded into an Argonaute (Ago) effector.
Seungjae Lee   +10 more
doaj   +1 more source

Biochemical Engineering Perspective on cGAS: From Enzyme Discovery to Potential Industrial Application. [PDF]

open access: yesChembiochem
This review examines the structural and enzymatic properties of cyclic GMP‐AMP synthase, including substrate promiscuity, homologs, and engineered variants. In addition, it evaluates potential expression systems for large‐scale enzyme production and analyzes reaction and purification strategies for the synthesis of cyclic dinucleotides to connect ...
Fataeri M, Rosenthal K.
europepmc   +2 more sources

A eubacterial origin for the human tRNA nucleotidyltransferase? [PDF]

open access: yes, 2001
tRNA CCA-termini are generated and maintained by tRNA nucleotidyltransferases. Together with poly(A) polymerases and other enzymes they belong to the nucleotidyltransferase superfamily.
Aebi M.   +12 more
core   +1 more source

Sequence motifs that distinguish ATP(CTP) : tRNA nucleotidyl transferases from eubacterial poly(A) polymerases [PDF]

open access: yes, 2004
ATP(CTP):tRNA nucleotidyl transferases, tRNA maturing enzymes found in all organisms, and eubacterial poly(A) polymerases, enzymes involved in mRNA degradation, are so similar that until now their biochemical functions could not be distinguished by their
Martin, G., Keller, W.
core   +1 more source

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