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3.1.13.1: exoribonuclease II

This is an abbreviated version!
For detailed information about exoribonuclease II, go to the full flat file.

Word Map on EC 3.1.13.1

Reaction

Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =

Synonyms

3'-5'exoribonuclease, 3’-5’exoribonuclease, 5'->3' exoribonuclease 2, AB205_0003320, Dis, Dis3, EC 3.1.4.20, exonuclease ISG20, More, PfRNase II, RC-RNase 2, ribonuclease 2, ribonuclease II, ribonuclease Q, Ribonuclease R, RNase, RNase 2, RNase A, RNase II, RNase R, RNase-2, RNaseR, Rnb, RNR, RNR1, Rrp44, XRN2

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.1 exoribonuclease II

Purification

Purification on EC 3.1.13.1 - exoribonuclease II

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
370fold, nearly to homogeneity
-
5300-26500fold, to homogeneity
-
all mutants, with the exception of R500K, by histidine affinity chromatography and the AKTA fast protein liquid chromatography system
anion exchange chromatography at denaturing conditions, in some cases followed by isoelectric focusing and dye binding chromatography
-
by affinity chromatography
-
by centrifugation, ion exchange and hydrophobic interaction chromatography
-
by histidine affinity chromatography and an AKTA HPLC system
Escherichia coli strain BL21(DE3)
-
full-length protein and mutants purified by affinity Ni-NTA chromatography, followed by ion exchange chromatography and gel filtration. 242-1001 construct purified to homogeneity
includes glutathione-Sepharose resin chromatography
-
partial purification that includes DEAE-Sepharose chromatography
-
partial purification, 500-700fold
-
partial purification, between 50-100fold
-
purification includes M2-agarose affinity resin
-
purified by inmunoprecipitation
-
purified on protein A-agarose and affinity GST-AtRrp4p inmobilized on nitrocellulose
-
recombinant His- or FLAG-tagged wild-type non-acetylated and acetylated and mutants from Escherichia coli strain BL21(DE3) by affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant RC-RNase 2 refolded from Escherichia coli strain BL21(DE3) inclusion bodies, further purification of the dialyzed enzyme by two different steps of cation exchange chromatography. The native enzyme is purified from oocytes by ultracentrifugation, extraction of the yolk granules from the pellet, followed by cation exchange chromatography
RNase R and RNase II constructs, full-length wild-type RNase R and RNase R mutant D278N
-
Rrp44-exosome (RE) architecture suggests an active site sequestration mechanism for strict control of 3' exoribonuclease activity in the RE complex
-
to apparent homogeneity, 270fold
-
wild-type and RNase II mutants purified by affinity chromatography