5'-Hydroxyl RNA kinase from mouse L cells.
A 5'-hydroxyl RNA kinase from mouse L cells has been partially purified and characterized. The enzyme transfers the gamma-phosphorus from ATP to 5'-hydroxyl termini of RNA much more efficiently than DNA substrates, and is virtually inactive on 3'-CMP. The molecular mass of the predominant kinase activity is estimated to be 93-96 kDa from denaturing and non-denaturing polyacrylamide gel analyses. A minor band of lower molecular mass has been also observed. The enzyme activity requires Mg2+ and is inhibited by both Mn2+ and Zn2+. Antibodies to small nuclear ribonucleoproteins have no effect on this activity.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D004722:Endoribonucleases; D007525:Isoelectric Focusing; D007739:L Cells / Q000201:enzymology; D051379:Mice; D009708:Nucleotidases; D010770:Phosphotransferases / Q000302:isolation & purification*; D011116:Polynucleotide 5'-Hydroxyl-Kinase / Q000302:isolation & purification*; D015719:Single-Strand Specific DNA and RNA Endonucleases; D013379:Substrate Specificity
D010770:Phosphotransferases; D011116:Polynucleotide 5'-Hydroxyl-Kinase; D004722:Endoribonucleases; C022543:ribonuclease T(2); D009708:Nucleotidases; D015719:Single-Strand Specific DNA and RNA Endonucleases