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Literature summary extracted from

  • Watkins, K.P.; Kroeger, T.S.; Cooke, A.M.; Williams-Carrier, R.E.; Friso, G.; Belcher, S.E.; van Wijk, K.J.; Barkan, A.
    A ribonuclease III domain protein functions in group II intron splicing in maize chloroplasts (2007), Plant Cell, 19, 2606-2623.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.3 into the pMAL-c2X vector, containing a TEV protease cleavage site at the EcoRI site, for expression in Escherichia coli Rosetta 2 cells Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.26.3 chloroplast
-
 Zea mays 9507
-
3.1.26.3 chloroplast stroma
-
 Zea mays 9570
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.3 Zea mays A6YSL1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.3 purified by affinity chromatography on amylose-coupled agarose resin, recombinant RNC1 binds RNA but lacks endonuclease activity Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.26.3 leaf
-
 Zea mays
-

Storage Stability

EC Number Storage Stability Organism
3.1.26.3 -20°C, 40 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, 5 mM 2-mercaptoethanol, 50% glycerol Zea mays

Synonyms

EC Number Synonyms Comment Organism
3.1.26.3 ribonuclease III
-
 Zea mays
3.1.26.3 RNase III
-
 Zea mays
3.1.26.3 RNC1 plant specific protein that contains two RNase III domains Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.3 25
-
 endonuclease assay Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.3 7.5
-
 endonuclease assay Zea mays