Results 31 to 40 of about 1,773 (158)
AGO-bound mature miRNAs are oligouridylated by TUTs and subsequently degraded by DIS3L2
Nature Communications, 2020 3′ end of microRNAs binds to the PAZ domain of Argonaute (AGO) proteins. Here the authors show that terminal nucleotidyltransferases TUT4/7 and exonuclease DIS3L2 induce tailing and decay of 3’ end exposed-microRNAs in AGO PAZ mutant expressing- or ...
Acong Yang +6 more
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A Phylogeny of Bacterial RNA Nucleotidyltransferases: Bacillus halodurans Contains Two tRNA Nucleotidyltransferases [PDF]
Journal of Bacteriology, 2005 ABSTRACT We have analyzed the distribution of RNA nucleotidyltransferases from the family that includes poly(A) polymerases (PAP) and tRNA nucleotidyltransferases (TNT) in 43 bacterial species. Genes of several bacterial species encode only one member of the nucleotidyltransferase superfamily (NTSF), and if that protein functions
Patricia, Bralley +2 more
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Purification and Characterization of a Mutant tRNA Nucleotidyltransferase [PDF]
European Journal of Biochemistry, 1980 tRNA nucleotidyltransferase has been extensively purified from a mutant strain of Escherichia coli which displays greatly decreased AMP incorporation, but normal CMP incorporation. The defect in AMP incorporation is retained throughout the purification of the mutant protein. The mutant protein behaves identically to the wild‐type protein with regard to
R G, McGann, M P, Deutscher
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Life, 2019 The early metabolism arising in a Thioester world gave rise to amino acids and their simple peptides. The catalytic activity of these early simple peptides became instrumental in the transition from Thioester World to a Phosphate World.
Hyman Hartman, Temple F. Smith
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Frontiers in Microbiology, 2023 BackgroundPaenibacillus thiaminolyticus, a species of genus Paenibacillus of the family Paenibacillaceae, exists widely in environments and habitats in various plants and worms, and occasionally causes human infections.
Junwan Lu +10 more
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TYMV RNA As a substrate of the tRNA nucleotidyltransferase [PDF]
FEBS Letters, 1970 It has been recently shown that in the presence of partly purified enzyme preparations from Escherichia coli and ATP. lhe RNA (M.W. = 2 × 106) of Turnip Yellow Mosaic Virus (TYMV) reacts with valine forming an ester bond analogous to that existing in aminoacyltRNA: lhe valine estcrifies the., -terminal adenosine ofTYMV RNA II. 21.
Litvak, S., Carré, D.S., Chapeville, F.
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THIOL GROUPS IN DEOXYRIBONUCLEIC ACID NUCLEOTIDYLTRANSFERASE [PDF]
Biochemical Journal, 1965 1. The inhibitory effects of iodoacetate, iodoacetamide, p-hydroxymercuribenzoate and sarkomycin were studied in a partially purified preparation of deoxyribonucleic acid nucleotidyltransferase from Landschutz ascites-tumour cells. All of these agents inhibited the activity of the enzyme, and it was shown that the inhibition exerted by the last three ...
H M, KEIR, J B, SHEPHERD
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Expanding the Substrate Scope of a Bacterial Nucleotidyltransferase via Allosteric Mutations
, 2022 Bacterial glycoconjugates, such as cell surface polysaccharides and glycoproteins, play important roles in cellular interactions and survival. Enzymes called nucleotidyltransferases use sugar-1-phosphates and nucleoside triphosphates (NTPs) to produce ...
Meng Zheng (1747132) +2 more
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The influence of spermidine on the reaction of RNA nucleotidyltransferase
Biochimica 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 ...
Petersen, E. E., Kroeger, H., Hagen, U.
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mBio, 2015 The aminoglycosides are highly effective broad-spectrum antimicrobial agents. However, their efficacy is diminished due to enzyme-mediated covalent modification, which reduces affinity of the drug for the target ribosome.
Georgina Cox +3 more
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