Results 121 to 130 of about 5,282 (158)
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Exoribonucleases and Endoribonucleases
EcoSal Plus, 2004This review provides a description of the known Escherichia coli ribonucleases (RNases), focusing on their structures, catalytic properties, genes, physiological roles, and possible regulation. Currently, eight E. coli exoribonucleases are known.
Murray P Deutscher
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Endoribonucleases associated with RNAs in chick embryos
proteins in hemopoietic rat cells were reported to have RNase activities [ 121. Similarly, an endogeneous endoribonucleolytic activity was found in the 50 S ribosomal subunit of Eschenihia coli [ 131. This paper describes the existence of a RNA-bound cytoplasmic endoribonuclease in chick embryo.
C D Denoya +2 more
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Chloroplast p54 Endoribonuclease
2001Publisher Summary Much of the regulation of chloroplast gene expression has been assigned to stability determinants at the level of RNA precursors, including interactions of sequence and/or structural elements with their cognate binding proteins. A number of these proteins are known to assemble at the 5′-untranslated region (UTR) of chloroplast mRNAs,
K, Liere, J, Nickelsen, G, Link
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Influenza Virus Endoribonuclease
2001The influenza virus polymerase complex contains two associated enzymatic activities, an endoribonuclease and a RNA-dependent RNA polymerase activity. Both activities have so far been observed only with the complete polymerase complex consisting of three subunits, PB1, PB2, and PA.
K, Klumpp, L, Hooker, B, Handa
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The role of endoribonucleases in the regulation of RNase R
Biochemical and Biophysical Research Communications, 2006RNase R is an important exoribonuclease involved in the maturation and degradation of RNA. RNase R is co-transcribed with other genes in the same operon. In this report, we show that under physiological conditions maturation of these co-transcripts and the levels of RNase R are mainly dependent on the endoribonuclease RNase E.
Fátima, Cairrão +1 more
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Endoribonucleases – enzymes gaining spotlight in mRNA metabolism
FEBS Journal, 2010The efficient turnover of messenger RNA represents an important mechanism that allows the cell to control gene expression. Until recently, the mechanism of mRNA decay was mainly attributed to exonucleases, comprising enzymes that degrade RNAs from the ends of the molecules.
Wai Ming Li, Chow H Lee
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Purification and characterization of a novel mammalian endoribonuclease
Journal of Cellular Biochemistry, 2005AbstractEndonuclease‐mediated mRNA decay appears to be a common mode of mRNA degradation in mammalian cells, but yet only a few mRNA endonucleases have been described. Here, we report the existence of a second mammalian endonuclease that is capable of cleaving c‐myc mRNA within the coding region in vitro.
Kirk, Bergstrom +4 more
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Endoribonuclease activities of Trypanosoma brucei mitochondria
Molecular and Biochemical Parasitology, 2002RNA editing in kinetoplastids is a type of post-transcriptional processing that changes mitochondrial mRNA sequences by the addition or deletion of uridines. Multiple enzymatic activities, such as endoribonuclease and RNA ligase, are associated with this process and exist in a multienzyme complex.
Reza, Salavati +5 more
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A microsomal endoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1980An endoribonuclease has been purified about 320-fold from the microsomes of rat liver. The enzyme had an apparent molecular weight of 54 000-58 000 and produced oligonucleotides, each consisting of 3-7 nucleotides from poly(A) and poly(U). No mononucleotide was obtained by the enzymatic hydrolysis of poly(A) and poly(U) under standard coditions.
H, Kumagai +5 more
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Characterization of an Endoribonuclease in Rat-Liver Nucleoli
European Journal of Biochemistry, 1974Synthetic RNAs, i.e. [3H]poly(U) and [14C]poly(A), and natural RNAs, i.e. 16-S and 23-S Escherichia coli ribosomal [14C]RNA and MS2 coliphage [3H]RNA, were incompletely hydrolyzed by a rat liver nucleolar enzyme as measured by solubilization of radioactivity following ethanol precipitation.
A, Boctor, A, Grossman, W, Szer
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