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Structures of 5′–3′ Exoribonucleases

2012
5'-3' Exoribonucleases (XRNs) have important functions in RNA processing, RNA turnover and decay, RNA interference, RNA polymerase transcription, and other cellular processes. Their sequences share two highly conserved regions, CR1 and CR2. The cytoplasmic Xrn1 and the nuclear Xrn2/Rat1 are found in yeast and animals, and XRNs are found in most other ...
Jeong Ho Chang, Song Xiang, Liang Tong
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5′-3′ Exoribonucleases

2011
The 5′-3′ exoribonucleases have important functions in RNA processing, RNA degradation, RNA interference, transcription, and other cellular processes. The Xrn1 and Xrn2/Rat1 family of enzymes are the best characterized 5′-3′ exoribonucleases, and there has been significant recent progress in the understanding of their structure and function. Especially,
Jeong Ho Chang   +3 more
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Drosophila 5′ → 3′-Exoribonuclease Pacman

2001
Publisher Summary This chapter concentrates on the methods used to express a Drosophila recombinat 5′ → 3′-exoribonuclease, purify the protein, and analyze its activity in vitro . Analysis of early development in Drosophila has shown that RNA localization, control of translation, and mRNA stability are intimately linked.
Sarah F. Newbury   +2 more
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Exoribonucleases and their multiple roles in RNA metabolism

2000
In recent years there has been a dramatic shift in our thinking about ribonucleases (RNases). Although they were once considered to be nonspecific, degradative enzymes, it is now clear that RNases play a central role in every aspect of cellular RNA metabolism, including decay of mRNA, conversion of RNA precursors to their mature forms, and end-turnover
Zhongwei Li, Murray P. Deutscher
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A cytoplasmic exoribonuclease from HeLa cells

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977
An exoribonuclease has been purified from the cytoplasm of HeLa cells. The enzyme produces 5'-AMP as the only product from poly(A). The degradation proceeds in a 3' to 5' direction, and a 3'-OH terminus is required. In addition to poly(A), the enzyme degrades other synthetic homopolymers as well as natural messenger, and ribosomal RNAs.
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Cooperation of Endo- and Exoribonucleases in Chloroplast mRNA Turnover

2004
Chloroplasts were acquired by eukaryotic cells through endosymbiosis and have retained their own gene expression machinery. One hallmark of chloroplast gene regulation is the predominance of posttranscriptional control, which is exerted both at the gene-specific and global levels.
Thomas J. Bollenbach   +2 more
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5′-Exoribonuclease 1: Xrn1

2001
Publisher Summary The detection, purification, and partial characterization of 5′-exoribonuclease 1 (Xrn1) from Saccharomyces cerevisiae as a 160-kDa RNase was reported in 1980 and 1985. The enzyme is a processive exonuclease hydrolyzing RNA from the 5′ end with the production of 5′-mononucleofides.
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Function and Characterization of Poly(A)-Specific 3´ Exoribonucleases

1997
Poly(A) tails are commonly found at the 3´ end of various classes of RNA (reviewed in Brawerman 1981; Manley 1995b). They are evolutionarily widespread and appear on RNAs of several different organisms. In mammalian cells almost all mRNAs end with an approximately 200-adenosine-residue-long poly(A) tail.
Jonas Åström, Anders Virtanen
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Chapter 9 In Vitro Assays of 5′ to 3′‐Exoribonuclease Activity

2008
The major cytoplasmic 5' to 3'-exoribonuclease activity is carried out by the Xrn1 protein in eukaryotic cells. A number of different approaches can be used to study multifunctional Xrn1 protein activity in vitro. In this chapter, we concentrate on methods used in our laboratory to analyze Xrn1 5' to 3'-exoribonuclease activity.
Pellegrini, O.   +3 more
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Simultaneous isolation of cytoplasmic endoribonuclease and exoribonuclease of Trypanosoma brucei

Molecular and Biochemical Parasitology, 1985
An endoribonuclease and an exoribonuclease have been isolated simultaneously from the cytoplasm of Trypanosoma brucei by hydroxyapatite column chromatography. The endoribonuclease produced oligonucleotides from poly(adenylic acid) with 5'-phosphate and 3'-OH termini. The exoribonuclease produced only ribonucleoside 5'-phosphates from poly(adenylic acid)
George O. Gbenle, George O. Gbenle
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