Secondary literature sources for EXOIII

The following references were automatically generated.

Barbas A, Matos RG, Amblar M, Lopez-Vinas E, Gomez-Puertas P, Arraiano CM
New insights into the mechanism of RNA degradation by ribonuclease II:identification of the residue responsible for setting the RNase II endproduct.
J Biol Chem. 2008; 283: 13070-6
Display abstract
RNase II is a key exoribonuclease involved in the maturation, turnover,and quality control of RNA. RNase II homologues are components of theexosome, a complex of exoribonucleases. The structure of RNase IIunraveled crucial aspects of the mechanism of RNA degradation. Here weshow that mutations in highly conserved residues at the active site affectthe activity of the enzyme. Moreover, we have identified the residue thatis responsible for setting the end product of RNase II. In addition, wepresent for the first time the models of two members of the RNase IIfamily, RNase R from Escherichia coli and human Rrp44, also called Dis3.Our findings improve the present model for RNA degradation by the RNase IIfamily of enzymes.

Li Z, Pandit S, Deutscher MP
3' exoribonucleolytic trimming is a common feature of the maturation ofsmall, stable RNAs in Escherichia coli.
Proc Natl Acad Sci U S A. 1998; 95: 2856-61
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In addition to tRNA and 5S RNA, Escherichia coli contains several othersmall, stable RNA species; these are M1, 10Sa, 6S, and 4.5S RNA. Althoughthese RNAs are initially synthesized as precursor molecules, relativelylittle is known about their maturation. The data presented here show that3' exoribonucleolytic trimming is required for the final maturation ofeach of these molecules. As found previously with tRNA, but not 5S RNA,any one of a number of exoribonucleases can carry out the trimmingreaction in vivo, although RNases T and PH are most effective. In theirabsence, large amounts of immature molecules accumulate for most of theRNAs, and these can be converted to the mature forms in vitro by thepurified RNases. A model is proposed that identifies a structural featurepresent in all the small, stable RNAs of E. coli, and describes how thisstructure together with the RNases influences the common mechanism for 3'maturation.

Aliotta JM, Pelletier JJ, Ware JL, Moran LS, Benner JS, Kong H
Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonucleaseactivity.
Genet Anal. 1996; 12: 185-95
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A thermostable DNA polymerase, the Bst DNA polymerase I, from Bacillusstearothermophilus N3468 was prepared to near-homogeneity. The dominantspecies of the Bst DNA polymerase I preparation sized about 97 kDa whenanalyzed on SDS polyacrylamide gels. The Bst polA gene that codes for Bstpolymerase I was cloned and sequenced. Comparative sequence analysisshowed that all three conserved 3'-->5' exonuclease motifs found in E.coli DNA polymerase I were missing in Bst DNA polymerase I. This castdoubt on the existence of a 3'-->5' exonuclease function in that enzyme.Four biochemical assays were used to measure exonuclease activities of BstDNA polymerase I, testing both full-length Bst polymerase I and the Bstlarge fragment which lacks the N-terminal 5'-->3' exonuclease domain.These exonuclease assays demonstrated that Bst DNA polymerase I onlycontained a double-strand dependent 5'-->3' exonuclease activity butlacked any detectable 3'-->5' proofreading exonuclease activity. The lackof 3'-->5' exonuclease function in a variety of thermostable repair DNApolymerases may reflect enhancement of thermostability at the expense ofproofreading activity.